3j63 - Revision history

OCA at 10:10, 21 February 2024

OCA — Wed, 21 Feb 2024 10:10:30 GMT

←Older revision		Revision as of 10:10, 21 February 2024
Line 9:		Line 9:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ASC_HUMAN ASC_HUMAN] Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.<ref>PMID:19759850</ref> <ref>PMID:11103777</ref> <ref>PMID:12486103</ref> <ref>PMID:12646168</ref> <ref>PMID:15030775</ref> <ref>PMID:14730312</ref> <ref>PMID:16585594</ref> <ref>PMID:16982856</ref> <ref>PMID:17599095</ref> <ref>PMID:17349957</ref> <ref>PMID:16964285</ref> <ref>PMID:19234215</ref> <ref>PMID:19494289</ref> <ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:20482797</ref> <ref>PMID:21487011</ref> <ref>PMID:22732093</ref> <ref>PMID:14499617</ref>		[https://www.uniprot.org/uniprot/ASC_HUMAN ASC_HUMAN] Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.<ref>PMID:19759850</ref> <ref>PMID:11103777</ref> <ref>PMID:12486103</ref> <ref>PMID:12646168</ref> <ref>PMID:15030775</ref> <ref>PMID:14730312</ref> <ref>PMID:16585594</ref> <ref>PMID:16982856</ref> <ref>PMID:17599095</ref> <ref>PMID:17349957</ref> <ref>PMID:16964285</ref> <ref>PMID:19234215</ref> <ref>PMID:19494289</ref> <ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:20482797</ref> <ref>PMID:21487011</ref> <ref>PMID:22732093</ref> <ref>PMID:14499617</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Inflammasomes elicit host defense inside cells by activating caspase-1 for cytokine maturation and cell death. AIM2 and NLRP3 are representative sensor proteins in two major families of inflammasomes. The adaptor protein ASC bridges the sensor proteins and caspase-1 to form ternary inflammasome complexes, achieved through pyrin domain (PYD) interactions between sensors and ASC and through caspase activation and recruitment domain (CARD) interactions between ASC and caspase-1. We found that PYD and CARD both form filaments. Activated AIM2 and NLRP3 nucleate PYD filaments of ASC, which, in turn, cluster the CARD of ASC. ASC thus nucleates CARD filaments of caspase-1, leading to proximity-induced activation. Endogenous NLRP3 inflammasome is also filamentous. The cryoelectron microscopy structure of ASC(PYD) filament at near-atomic resolution provides a template for homo- and hetero-PYD/PYD associations, as confirmed by structure-guided mutagenesis. We propose that ASC-dependent inflammasomes in both families share a unified assembly mechanism that involves two successive steps of nucleation-induced polymerization. PAPERFLICK:
-
-	Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes.,Lu A, Magupalli VG, Ruan J, Yin Q, Atianand MK, Vos MR, Schroder GF, Fitzgerald KA, Wu H, Egelman EH Cell. 2014 Mar 13;156(6):1193-206. doi: 10.1016/j.cell.2014.02.008. PMID:24630722<ref>PMID:24630722</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3j63" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:16, 24 January 2024

OCA — Wed, 24 Jan 2024 14:16:07 GMT

←Older revision		Revision as of 14:16, 24 January 2024
Line 3:		Line 3:
	<SX load='3j63' size='340' side='right' viewer='molstar' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>		<SX load='3j63' size='340' side='right' viewer='molstar' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J63 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J63 FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~PYCARD~~, ~~ASC, CARD5, TMS1 (~~[~~https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 3.8Å</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j63 OCA], [https://pdbe.org/3j63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j63 RCSB], [https://www.ebi.ac.uk/pdbsum/3j63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j63 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j63 OCA], [https://pdbe.org/3j63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j63 RCSB], [https://www.ebi.ac.uk/pdbsum/3j63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j63 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ASC_HUMAN ASC_HUMAN]] Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.<ref>PMID:19759850</ref> <ref>PMID:11103777</ref> <ref>PMID:12486103</ref> <ref>PMID:12646168</ref> <ref>PMID:15030775</ref> <ref>PMID:14730312</ref> <ref>PMID:16585594</ref> <ref>PMID:16982856</ref> <ref>PMID:17599095</ref> <ref>PMID:17349957</ref> <ref>PMID:16964285</ref> <ref>PMID:19234215</ref> <ref>PMID:19494289</ref> <ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:20482797</ref> <ref>PMID:21487011</ref> <ref>PMID:22732093</ref> <ref>PMID:14499617</ref>	+	[https://www.uniprot.org/uniprot/ASC_HUMAN ASC_HUMAN] Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.<ref>PMID:19759850</ref> <ref>PMID:11103777</ref> <ref>PMID:12486103</ref> <ref>PMID:12646168</ref> <ref>PMID:15030775</ref> <ref>PMID:14730312</ref> <ref>PMID:16585594</ref> <ref>PMID:16982856</ref> <ref>PMID:17599095</ref> <ref>PMID:17349957</ref> <ref>PMID:16964285</ref> <ref>PMID:19234215</ref> <ref>PMID:19494289</ref> <ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:20482797</ref> <ref>PMID:21487011</ref> <ref>PMID:22732093</ref> <ref>PMID:14499617</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Atianand~~, M K~~]]	+	[[Category: Atianand MK]]
-	[[Category: Egelman~~, E H~~]]	+	[[Category: Egelman EH]]
-	[[Category: Fitzgerald~~, K A~~]]	+	[[Category: Fitzgerald KA]]
-	[[Category: Lu, A]]	+	[[Category: Lu A]]
-	[[Category: Magupalli~~, V G~~]]	+	[[Category: Magupalli VG]]
-	[[Category: Ruan, J]]	+	[[Category: Ruan J]]
-	[[Category: Schroder~~, G F~~]]	+	[[Category: Schroder GF]]
-	[[Category: Vos, M]]	+	[[Category: Vos M]]
-	[[Category: Wu, H]]	+	[[Category: Wu H]]
-	[[Category: Yin, Q]]	+	[[Category: Yin Q]]
-	~~[[Category: Apoptosis]]~~	+
-	~~[[Category: Death domain]]~~	+
-	~~[[Category: Helical polymer]]~~	+
-	~~[[Category: Variable twist~~]]	+

OCA at 03:50, 21 April 2022

OCA — Thu, 21 Apr 2022 03:50:25 GMT

←Older revision		Revision as of 03:50, 21 April 2022
Line 3:		Line 3:
	<SX load='3j63' size='340' side='right' viewer='molstar' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>		<SX load='3j63' size='340' side='right' viewer='molstar' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3J63 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J63 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PYCARD, ASC, CARD5, TMS1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PYCARD, ASC, CARD5, TMS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=3j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j63 OCA], [~~http~~://pdbe.org/3j63 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3j63 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3j63 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3j63 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j63 OCA], [https://pdbe.org/3j63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j63 RCSB], [https://www.ebi.ac.uk/pdbsum/3j63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j63 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ASC_HUMAN ASC_HUMAN]] Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.<ref>PMID:19759850</ref> <ref>PMID:11103777</ref> <ref>PMID:12486103</ref> <ref>PMID:12646168</ref> <ref>PMID:15030775</ref> <ref>PMID:14730312</ref> <ref>PMID:16585594</ref> <ref>PMID:16982856</ref> <ref>PMID:17599095</ref> <ref>PMID:17349957</ref> <ref>PMID:16964285</ref> <ref>PMID:19234215</ref> <ref>PMID:19494289</ref> <ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:20482797</ref> <ref>PMID:21487011</ref> <ref>PMID:22732093</ref> <ref>PMID:14499617</ref>	+	[[https://www.uniprot.org/uniprot/ASC_HUMAN ASC_HUMAN]] Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.<ref>PMID:19759850</ref> <ref>PMID:11103777</ref> <ref>PMID:12486103</ref> <ref>PMID:12646168</ref> <ref>PMID:15030775</ref> <ref>PMID:14730312</ref> <ref>PMID:16585594</ref> <ref>PMID:16982856</ref> <ref>PMID:17599095</ref> <ref>PMID:17349957</ref> <ref>PMID:16964285</ref> <ref>PMID:19234215</ref> <ref>PMID:19494289</ref> <ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:20482797</ref> <ref>PMID:21487011</ref> <ref>PMID:22732093</ref> <ref>PMID:14499617</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:58, 10 April 2020

OCA — Fri, 10 Apr 2020 17:58:42 GMT

←Older revision		Revision as of 17:58, 10 April 2020
Line 3:		Line 3:
	<SX load='3j63' size='340' side='right' viewer='molstar' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>		<SX load='3j63' size='340' side='right' viewer='molstar' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3J63 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3J63 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PYCARD, ASC, CARD5, TMS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PYCARD, ASC, CARD5, TMS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j63 OCA], [http://pdbe.org/3j63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j63 RCSB], [http://www.ebi.ac.uk/pdbsum/3j63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j63 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j63 OCA], [http://pdbe.org/3j63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j63 RCSB], [http://www.ebi.ac.uk/pdbsum/3j63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j63 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 17:25, 6 March 2020

OCA — Fri, 06 Mar 2020 17:25:01 GMT

←Older revision		Revision as of 17:25, 6 March 2020
Line 1:		Line 1:

	==Unified assembly mechanism of ASC-dependent inflammasomes==		==Unified assembly mechanism of ASC-dependent inflammasomes==
-	<~~StructureSection~~ load='3j63' size='340' side='right' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>	+	<SX load='3j63' size='340' side='right' viewer='molstar' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J63 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J63 FirstGlance]. <br>
Line 21:		Line 21:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Atianand, M K]]		[[Category: Atianand, M K]]
	[[Category: Egelman, E H]]		[[Category: Egelman, E H]]

OCA at 14:17, 4 August 2016

OCA — Thu, 04 Aug 2016 14:17:53 GMT

←Older revision		Revision as of 14:17, 4 August 2016
Line 1:		Line 1:
		+
	==Unified assembly mechanism of ASC-dependent inflammasomes==		==Unified assembly mechanism of ASC-dependent inflammasomes==
	<StructureSection load='3j63' size='340' side='right' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>		<StructureSection load='3j63' size='340' side='right' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J63 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J63 FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PYCARD, ASC, CARD5, TMS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PYCARD, ASC, CARD5, TMS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j63 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j63 RCSB], [http://www.ebi.ac.uk/pdbsum/3j63 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j63 OCA], [http://pdbe.org/3j63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j63 RCSB], [http://www.ebi.ac.uk/pdbsum/3j63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j63 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3j63" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:32, 24 December 2014

OCA — Wed, 24 Dec 2014 15:32:27 GMT

←Older revision		Revision as of 15:32, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3j63\| PDB=3j63 \| SCENE= }}~~	+	==Unified assembly mechanism of ASC-dependent inflammasomes==
-	===Unified assembly mechanism of ASC-dependent inflammasomes===	+	<StructureSection load='3j63' size='340' side='right' caption='[[3j63]], [[Resolution\|resolution]] 3.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24630722}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3j63]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J63 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PYCARD, ASC, CARD5, TMS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j63 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j63 RCSB], [http://www.ebi.ac.uk/pdbsum/3j63 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/ASC_HUMAN ASC_HUMAN]] Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.<ref>PMID:19759850</ref> <ref>PMID:11103777</ref> <ref>PMID:12486103</ref> <ref>PMID:12646168</ref> <ref>PMID:15030775</ref> <ref>PMID:14730312</ref> <ref>PMID:16585594</ref> <ref>PMID:16982856</ref> <ref>PMID:17599095</ref> <ref>PMID:17349957</ref> <ref>PMID:16964285</ref> <ref>PMID:19234215</ref> <ref>PMID:19494289</ref> <ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:20482797</ref> <ref>PMID:21487011</ref> <ref>PMID:22732093</ref> <ref>PMID:14499617</ref>		[[http://www.uniprot.org/uniprot/ASC_HUMAN ASC_HUMAN]] Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.<ref>PMID:19759850</ref> <ref>PMID:11103777</ref> <ref>PMID:12486103</ref> <ref>PMID:12646168</ref> <ref>PMID:15030775</ref> <ref>PMID:14730312</ref> <ref>PMID:16585594</ref> <ref>PMID:16982856</ref> <ref>PMID:17599095</ref> <ref>PMID:17349957</ref> <ref>PMID:16964285</ref> <ref>PMID:19234215</ref> <ref>PMID:19494289</ref> <ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:20482797</ref> <ref>PMID:21487011</ref> <ref>PMID:22732093</ref> <ref>PMID:14499617</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Inflammasomes elicit host defense inside cells by activating caspase-1 for cytokine maturation and cell death. AIM2 and NLRP3 are representative sensor proteins in two major families of inflammasomes. The adaptor protein ASC bridges the sensor proteins and caspase-1 to form ternary inflammasome complexes, achieved through pyrin domain (PYD) interactions between sensors and ASC and through caspase activation and recruitment domain (CARD) interactions between ASC and caspase-1. We found that PYD and CARD both form filaments. Activated AIM2 and NLRP3 nucleate PYD filaments of ASC, which, in turn, cluster the CARD of ASC. ASC thus nucleates CARD filaments of caspase-1, leading to proximity-induced activation. Endogenous NLRP3 inflammasome is also filamentous. The cryoelectron microscopy structure of ASC(PYD) filament at near-atomic resolution provides a template for homo- and hetero-PYD/PYD associations, as confirmed by structure-guided mutagenesis. We propose that ASC-dependent inflammasomes in both families share a unified assembly mechanism that involves two successive steps of nucleation-induced polymerization. PAPERFLICK:

-	~~==About this Structure==~~	+	Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes.,Lu A, Magupalli VG, Ruan J, Yin Q, Atianand MK, Vos MR, Schroder GF, Fitzgerald KA, Wu H, Egelman EH Cell. 2014 Mar 13;156(6):1193-206. doi: 10.1016/j.cell.2014.02.008. PMID:24630722<ref>PMID:24630722</ref>
-	~~[[3j63]] is a 15 chain structure~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.~~il/oca-bin/ocashort?id=3J63 OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024630722</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
-	[[Category: Atianand, M K.]]	+	== References ==
-	[[Category: Egelman, E H.]]	+	<references/>
-	[[Category: Fitzgerald, K A.]]	+	__TOC__
-	[[Category: Lu, A.]]	+	</StructureSection>
-	[[Category: Magupalli, V G.]]	+	[[Category: Human]]
-	[[Category: Ruan, J.]]	+	[[Category: Atianand, M K]]
-	[[Category: Schroder, G F.]]	+	[[Category: Egelman, E H]]
-	[[Category: Vos, M.]]	+	[[Category: Fitzgerald, K A]]
-	[[Category: Wu, H.]]	+	[[Category: Lu, A]]
-	[[Category: Yin, Q.]]	+	[[Category: Magupalli, V G]]
		+	[[Category: Ruan, J]]
		+	[[Category: Schroder, G F]]
		+	[[Category: Vos, M]]
		+	[[Category: Wu, H]]
		+	[[Category: Yin, Q]]
	[[Category: Apoptosis]]		[[Category: Apoptosis]]
	[[Category: Death domain]]		[[Category: Death domain]]
	[[Category: Helical polymer]]		[[Category: Helical polymer]]
	[[Category: Variable twist]]		[[Category: Variable twist]]

OCA at 09:19, 26 March 2014

OCA — Wed, 26 Mar 2014 09:19:32 GMT

←Older revision		Revision as of 09:19, 26 March 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_3j63\| PDB=3j63 \| SCENE= }}
		+	===Unified assembly mechanism of ASC-dependent inflammasomes===
		+	{{ABSTRACT_PUBMED_24630722}}

-	The ~~entry 3j63~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/ASC_HUMAN ASC_HUMAN]] Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.<ref>PMID:19759850</ref> <ref>PMID:11103777</ref> <ref>PMID:12486103</ref> <ref>PMID:12646168</ref> <ref>PMID:15030775</ref> <ref>PMID:14730312</ref> <ref>PMID:16585594</ref> <ref>PMID:16982856</ref> <ref>PMID:17599095</ref> <ref>PMID:17349957</ref> <ref>PMID:16964285</ref> <ref>PMID:19234215</ref> <ref>PMID:19494289</ref> <ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:20482797</ref> <ref>PMID:21487011</ref> <ref>PMID:22732093</ref> <ref>PMID:14499617</ref>

-	~~Authors~~: ~~Lu, A., Magupalli, V.G., Ruan, J., Yin, Q., Atianand, M.K., Vos, M., Schroder, G.F., Fitzgerald, K.A~~.~~, Wu, H~~.~~, Egelman, E~~.H.	+	==About this Structure==
		+	[[3j63]] is a 15 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J63 OCA].

-	~~Description~~: ~~Unified assembly mechanism of ASC-dependent inflammasomes~~	+	==Reference==
		+	<ref group="xtra">PMID:024630722</ref><references group="xtra"/><references/>
		+	[[Category: Atianand, M K.]]
		+	[[Category: Egelman, E H.]]
		+	[[Category: Fitzgerald, K A.]]
		+	[[Category: Lu, A.]]
		+	[[Category: Magupalli, V G.]]
		+	[[Category: Ruan, J.]]
		+	[[Category: Schroder, G F.]]
		+	[[Category: Vos, M.]]
		+	[[Category: Wu, H.]]
		+	[[Category: Yin, Q.]]
		+	[[Category: Apoptosis]]
		+	[[Category: Death domain]]
		+	[[Category: Helical polymer]]
		+	[[Category: Variable twist]]

OCA at 08:36, 8 January 2014

OCA — Wed, 08 Jan 2014 08:36:47 GMT

←Older revision		Revision as of 08:36, 8 January 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3j63 is ON HOLD	+	The entry 3j63 is ON HOLD until Paper Publication

	Authors: Lu, A., Magupalli, V.G., Ruan, J., Yin, Q., Atianand, M.K., Vos, M., Schroder, G.F., Fitzgerald, K.A., Wu, H., Egelman, E.H.		Authors: Lu, A., Magupalli, V.G., Ruan, J., Yin, Q., Atianand, M.K., Vos, M., Schroder, G.F., Fitzgerald, K.A., Wu, H., Egelman, E.H.

	Description: Unified assembly mechanism of ASC-dependent inflammasomes		Description: Unified assembly mechanism of ASC-dependent inflammasomes

OCA: Protected "3j63" [edit=sysop:move=sysop]

OCA — Wed, 11 Dec 2013 12:41:10 GMT

Protected "3j63" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:41, 11 December 2013