6dce

From Proteopedia

(Difference between revisions)

Current revision

X-ray structure of FIP200 claw domain

Structural highlights

6dce is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.56Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RBCC1_HUMAN Involved in autophagy (PubMed:21775823). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (By similarity). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (PubMed:10769033, PubMed:12221124). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (By similarity). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:14533007). Plays a crucial role in muscular differentiation (PubMed:12163359). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity).[UniProtKB:Q9ESK9]^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

The autophagy cargo receptor p62 facilitates the condensation of misfolded, ubiquitin-positive proteins and their degradation by autophagy, but the molecular mechanism of p62 signaling to the core autophagy machinery is unclear. Here, we show that disordered residues 326-380 of p62 directly interact with the C-terminal region (CTR) of FIP200. Crystal structure determination shows that the FIP200 CTR contains a dimeric globular domain that we designated the "Claw" for its shape. The interaction of p62 with FIP200 is mediated by a positively charged pocket in the Claw, enhanced by p62 phosphorylation, mutually exclusive with the binding of p62 to LC3B, and it promotes degradation of ubiquitinated cargo by autophagy. Furthermore, the recruitment of the FIP200 CTR slows the phase separation of ubiquitinated proteins by p62 in a reconstituted system. Our data provide the molecular basis for a crosstalk between cargo condensation and autophagosome formation.

FIP200 Claw Domain Binding to p62 Promotes Autophagosome Formation at Ubiquitin Condensates.,Turco E, Witt M, Abert C, Bock-Bierbaum T, Su MY, Trapannone R, Sztacho M, Danieli A, Shi X, Zaffagnini G, Gamper A, Schuschnig M, Fracchiolla D, Bernklau D, Romanov J, Hartl M, Hurley JH, Daumke O, Martens S Mol Cell. 2019 Feb 26. pii: S1097-2765(19)30055-3. doi:, 10.1016/j.molcel.2019.01.035. PMID:30853400^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ueda H, Abbi S, Zheng C, Guan JL. Suppression of Pyk2 kinase and cellular activities by FIP200. J Cell Biol. 2000 Apr 17;149(2):423-30. PMID:10769033
↑ Chano T, Ikegawa S, Saito-Ohara F, Inazawa J, Mabuchi A, Saeki Y, Okabe H. Isolation, characterization and mapping of the mouse and human RB1CC1 genes. Gene. 2002 May 29;291(1-2):29-34. PMID:12095676
↑ Chano T, Saeki Y, Serra M, Matsumoto K, Okabe H. Preferential expression of RB1-inducible coiled-coil 1 in terminal differentiated musculoskeletal cells. Am J Pathol. 2002 Aug;161(2):359-64. doi: 10.1016/S0002-9440(10)64190-9. PMID:12163359 doi:http://dx.doi.org/10.1016/S0002-9440(10)64190-9
↑ Abbi S, Ueda H, Zheng C, Cooper LA, Zhao J, Christopher R, Guan JL. Regulation of focal adhesion kinase by a novel protein inhibitor FIP200. Mol Biol Cell. 2002 Sep;13(9):3178-91. doi: 10.1091/mbc.e02-05-0295. PMID:12221124 doi:http://dx.doi.org/10.1091/mbc.e02-05-0295
↑ Kontani K, Chano T, Ozaki Y, Tezuka N, Sawai S, Fujino S, Saeki Y, Okabe H. RB1CC1 suppresses cell cycle progression through RB1 expression in human neoplastic cells. Int J Mol Med. 2003 Nov;12(5):767-9. PMID:14533007
↑ Morselli E, Shen S, Ruckenstuhl C, Bauer MA, Marino G, Galluzzi L, Criollo A, Michaud M, Maiuri MC, Chano T, Madeo F, Kroemer G. p53 inhibits autophagy by interacting with the human ortholog of yeast Atg17, RB1CC1/FIP200. Cell Cycle. 2011 Aug 15;10(16):2763-9. doi: 10.4161/cc.10.16.16868. Epub 2011 Aug, 15. PMID:21775823 doi:http://dx.doi.org/10.4161/cc.10.16.16868
↑ Nishimura T, Kaizuka T, Cadwell K, Sahani MH, Saitoh T, Akira S, Virgin HW, Mizushima N. FIP200 regulates targeting of Atg16L1 to the isolation membrane. EMBO Rep. 2013 Mar 1;14(3):284-91. doi: 10.1038/embor.2013.6. Epub 2013 Feb 8. PMID:23392225 doi:http://dx.doi.org/10.1038/embor.2013.6
↑ Turco E, Witt M, Abert C, Bock-Bierbaum T, Su MY, Trapannone R, Sztacho M, Danieli A, Shi X, Zaffagnini G, Gamper A, Schuschnig M, Fracchiolla D, Bernklau D, Romanov J, Hartl M, Hurley JH, Daumke O, Martens S. FIP200 Claw Domain Binding to p62 Promotes Autophagosome Formation at Ubiquitin Condensates. Mol Cell. 2019 Feb 26. pii: S1097-2765(19)30055-3. doi:, 10.1016/j.molcel.2019.01.035. PMID:30853400 doi:http://dx.doi.org/10.1016/j.molcel.2019.01.035

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6dce"

Categories: Homo sapiens | Large Structures | Hurley JH | Su M-Y

@@ Line 3: / Line 3: @@
 <StructureSection load='6dce' size='340' side='right'caption='[[6dce]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6dce]] is a 1 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=6DCE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DCE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6dce]] is a 1 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=6DCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DCE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RB1CC1, KIAA0203, RBICC ([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'>[https://proteopedia.org/fgij/fg.htm?mol=6dce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dce OCA], [https://pdbe.org/6dce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dce RCSB], [https://www.ebi.ac.uk/pdbsum/6dce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dce ProSAT]</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=6dce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dce OCA], [http://pdbe.org/6dce PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dce RCSB], [http://www.ebi.ac.uk/pdbsum/6dce PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dce ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RBCC1_HUMAN RBCC1_HUMAN]] Involved in autophagy (PubMed:21775823). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (By similarity). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (PubMed:10769033, PubMed:12221124). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (By similarity). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:14533007). Plays a crucial role in muscular differentiation (PubMed:12163359). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity).[UniProtKB:Q9ESK9]<ref>PMID:10769033</ref> <ref>PMID:12095676</ref> <ref>PMID:12163359</ref> <ref>PMID:12221124</ref> <ref>PMID:14533007</ref> <ref>PMID:21775823</ref> <ref>PMID:23392225</ref>
+[https://www.uniprot.org/uniprot/RBCC1_HUMAN RBCC1_HUMAN] Involved in autophagy (PubMed:21775823). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (By similarity). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (PubMed:10769033, PubMed:12221124). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (By similarity). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:14533007). Plays a crucial role in muscular differentiation (PubMed:12163359). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity).[UniProtKB:Q9ESK9]<ref>PMID:10769033</ref> <ref>PMID:12095676</ref> <ref>PMID:12163359</ref> <ref>PMID:12221124</ref> <ref>PMID:14533007</ref> <ref>PMID:21775823</ref> <ref>PMID:23392225</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Hurley, J H]]
+[[Category: Hurley JH]]
-[[Category: Su, M Y]]
+[[Category: Su M-Y]]
-[[Category: Autophagy]]
-[[Category: Fip200]]
-[[Category: Structural protein]]

6dce

From Proteopedia

Current revision

X-ray structure of FIP200 claw domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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