5wrk - Revision history

OCA at 16:51, 8 November 2023

OCA — Wed, 08 Nov 2023 16:51:59 GMT

←Older revision		Revision as of 16:51, 8 November 2023
Line 1:		Line 1:

	==Mu2 subunit of the clathrin adaptor complex AP2 in complex with IRS-1 Y608 peptide==		==Mu2 subunit of the clathrin adaptor complex AP2 in complex with IRS-1 Y608 peptide==
-	<StructureSection load='5wrk' size='340' side='right' caption='[[5wrk]], [[Resolution\|resolution]] 2.62Å' scene=''>	+	<StructureSection load='5wrk' size='340' side='right'caption='[[5wrk]], [[Resolution\|resolution]] 2.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5wrk]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5WRK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5wrk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WRK FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 2.62Å</td></tr>
-	~~<tr~~ id~~='NonStdRes'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Non-Standard_Residue~~\|~~NonStd Res:~~]]~~</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[5wrl\|5wrl]], [[5wrm\|5wrm]]</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=5wrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrk OCA], [https://pdbe.org/5wrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wrk RCSB], [https://www.ebi.ac.uk/pdbsum/5wrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrk ProSAT]</span></td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~"><~~b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">Ap2m1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])~~</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=5wrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrk OCA], [~~http~~://pdbe.org/5wrk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5wrk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5wrk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrk ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/AP2M1_RAT AP2M1_RAT]] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling.<ref>PMID:11516654</ref> <ref>PMID:14745134</ref> <ref>PMID:15473838</ref> <ref>PMID:20947020</ref> [[http://www.uniprot.org/uniprot/IRS1_RAT IRS1_RAT]] May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit.<ref>PMID:1380456</ref>	+	[https://www.uniprot.org/uniprot/AP2M1_RAT AP2M1_RAT] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling.<ref>PMID:11516654</ref> <ref>PMID:14745134</ref> <ref>PMID:15473838</ref> <ref>PMID:20947020</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5wrk" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5wrk" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Adaptin 3D structures\|Adaptin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buffalo rat~~]]	+	[[Category: Large Structures]]
-	[[Category: Hakuno, F]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Niwa, H]]	+	[[Category: Hakuno F]]
-	[[Category: Takahashi, S]]	+	[[Category: Niwa H]]
-	[[Category: Umehara, T]]	+	[[Category: Takahashi S]]
-	[[Category: Yokoyama, S]]	+	[[Category: Umehara T]]
-	[[Category: Yoneyama, Y]]	+	[[Category: Yokoyama S]]
-	~~[[Category: Clathrin adaptor ap-2 complex subunit]]~~	+	[[Category: Yoneyama Y]]
-	~~[[Category: Endocytosis]]~~	+
-	~~[[Category: Peptide complex~~]]	+

OCA at 08:44, 19 December 2018

OCA — Wed, 19 Dec 2018 08:44:19 GMT

←Older revision		Revision as of 08:44, 19 December 2018
Line 3:		Line 3:
	<StructureSection load='5wrk' size='340' side='right' caption='[[5wrk]], [[Resolution\|resolution]] 2.62Å' scene=''>		<StructureSection load='5wrk' size='340' side='right' caption='[[5wrk]], [[Resolution\|resolution]] 2.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5wrk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WRK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5wrk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WRK FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5wrl\|5wrl]], [[5wrm\|5wrm]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5wrl\|5wrl]], [[5wrm\|5wrm]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Ap2m1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=5wrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrk OCA], [http://pdbe.org/5wrk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wrk RCSB], [http://www.ebi.ac.uk/pdbsum/5wrk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrk 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=5wrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrk OCA], [http://pdbe.org/5wrk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wrk RCSB], [http://www.ebi.ac.uk/pdbsum/5wrk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/AP2M1_RAT AP2M1_RAT]] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling.<ref>PMID:11516654</ref> <ref>PMID:14745134</ref> <ref>PMID:15473838</ref> <ref>PMID:20947020</ref> [[http://www.uniprot.org/uniprot/IRS1_RAT IRS1_RAT]] May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit.<ref>PMID:1380456</ref>		[[http://www.uniprot.org/uniprot/AP2M1_RAT AP2M1_RAT]] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling.<ref>PMID:11516654</ref> <ref>PMID:14745134</ref> <ref>PMID:15473838</ref> <ref>PMID:20947020</ref> [[http://www.uniprot.org/uniprot/IRS1_RAT IRS1_RAT]] May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit.<ref>PMID:1380456</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Insulin-like growth factor-I receptor (IGF-IR) preferentially regulates the long-term IGF activities including growth and metabolism. Kinetics of ligand-dependent IGF-IR endocytosis determines how IGF induces such downstream signaling outputs. Here, we find that the insulin receptor substrate (IRS)-1 modulates how long ligand-activated IGF-IR remains at the cell surface before undergoing endocytosis in mammalian cells. IRS-1 interacts with the clathrin adaptor complex AP2. IRS-1, but not an AP2-binding-deficient mutant, delays AP2-mediated IGF-IR endocytosis after the ligand stimulation. Mechanistically, IRS-1 inhibits the recruitment of IGF-IR into clathrin-coated structures; for this reason, IGF-IR avoids rapid endocytosis and prolongs its activity on the cell surface. Accelerating IGF-IR endocytosis via IRS-1 depletion induces the shift from sustained to transient Akt activation and augments FoxO-mediated transcription. Our study establishes a new role for IRS-1 as an endocytic regulator of IGF-IR that ensures sustained IGF bioactivity, independent of its classic role as an adaptor in IGF-IR signaling.
		+
		+	IRS-1 acts as an endocytic regulator of IGF-I receptor to facilitate sustained IGF signaling.,Yoneyama Y, Lanzerstorfer P, Niwa H, Umehara T, Shibano T, Yokoyama S, Chida K, Weghuber J, Hakuno F, Takahashi SI Elife. 2018 Apr 11;7. pii: 32893. doi: 10.7554/eLife.32893. PMID:29661273<ref>PMID:29661273</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5wrk" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Hakuno, F]]		[[Category: Hakuno, F]]
	[[Category: Niwa, H]]		[[Category: Niwa, H]]

OCA at 07:18, 6 December 2017

OCA — Wed, 06 Dec 2017 07:18:43 GMT

←Older revision		Revision as of 07:18, 6 December 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5wrk is ~~ON HOLD until Paper Publication~~	+	==Mu2 subunit of the clathrin adaptor complex AP2 in complex with IRS-1 Y608 peptide==
-		+	<StructureSection load='5wrk' size='340' side='right' caption='[[5wrk]], [[Resolution\|resolution]] 2.62Å' scene=''>
-	~~Authors~~: ~~Yoneyama~~, Y.~~, Niwa, H~~., ~~Umehara~~, T., ~~Yokoyama, S~~., ~~Hakuno, F~~., ~~Takahashi, S~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5wrk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WRK FirstGlance]. <br>
-	~~Description~~: ~~Mu2 subunit~~ of the ~~clathrin~~ adaptor complex ~~AP2~~ in ~~complex~~ with ~~IRS~~-~~1 Y608 peptide~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
-	[[~~Category: Unreleased Structures~~]]	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
-	[[~~Category~~: ~~Takahashi, S~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5wrl\|5wrl]], [[5wrm\|5wrm]]</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=5wrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrk OCA], [http://pdbe.org/5wrk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wrk RCSB], [http://www.ebi.ac.uk/pdbsum/5wrk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrk ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AP2M1_RAT AP2M1_RAT]] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling.<ref>PMID:11516654</ref> <ref>PMID:14745134</ref> <ref>PMID:15473838</ref> <ref>PMID:20947020</ref> [[http://www.uniprot.org/uniprot/IRS1_RAT IRS1_RAT]] May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit.<ref>PMID:1380456</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Hakuno, F]]		[[Category: Hakuno, F]]
	[[Category: Niwa, H]]		[[Category: Niwa, H]]
		+	[[Category: Takahashi, S]]
	[[Category: Umehara, T]]		[[Category: Umehara, T]]
	[[Category: Yokoyama, S]]		[[Category: Yokoyama, S]]
	[[Category: Yoneyama, Y]]		[[Category: Yoneyama, Y]]
		+	[[Category: Clathrin adaptor ap-2 complex subunit]]
		+	[[Category: Endocytosis]]
		+	[[Category: Peptide complex]]

OCA at 04:53, 29 November 2017

OCA — Wed, 29 Nov 2017 04:53:12 GMT

←Older revision		Revision as of 04:53, 29 November 2017
Line 5:		Line 5:
	Authors: Yoneyama, Y., Niwa, H., Umehara, T., Yokoyama, S., Hakuno, F., Takahashi, S.		Authors: Yoneyama, Y., Niwa, H., Umehara, T., Yokoyama, S., Hakuno, F., Takahashi, S.

-	Description: ~~protein~~ in complex with ~~peptide (~~Y608)	+	Description: Mu2 subunit of the clathrin adaptor complex AP2 in complex with IRS-1 Y608 peptide
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Takahashi, S]]
		+	[[Category: Hakuno, F]]
	[[Category: Niwa, H]]		[[Category: Niwa, H]]
	[[Category: Umehara, T]]		[[Category: Umehara, T]]
	[[Category: Yokoyama, S]]		[[Category: Yokoyama, S]]
	[[Category: Yoneyama, Y]]		[[Category: Yoneyama, Y]]
-	[[Category: Hakuno, F]]
-	[[Category: Takahashi, S]]

OCA at 15:05, 27 September 2017

OCA — Wed, 27 Sep 2017 15:05:44 GMT

←Older revision		Revision as of 15:05, 27 September 2017
Line 7:		Line 7:
	Description: protein in complex with peptide (Y608)		Description: protein in complex with peptide (Y608)
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Hakuno, F]]
	[[Category: Niwa, H]]		[[Category: Niwa, H]]
-	[[Category: Takahashi, S]]
	[[Category: Umehara, T]]		[[Category: Umehara, T]]
	[[Category: Yokoyama, S]]		[[Category: Yokoyama, S]]
	[[Category: Yoneyama, Y]]		[[Category: Yoneyama, Y]]
		+	[[Category: Hakuno, F]]
		+	[[Category: Takahashi, S]]

OCA at 19:48, 15 March 2017

OCA — Wed, 15 Mar 2017 19:48:34 GMT

←Older revision		Revision as of 19:48, 15 March 2017
Line 7:		Line 7:
	Description: protein in complex with peptide (Y608)		Description: protein in complex with peptide (Y608)
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Hakuno, F]]
	[[Category: Niwa, H]]		[[Category: Niwa, H]]
		+	[[Category: Takahashi, S]]
	[[Category: Umehara, T]]		[[Category: Umehara, T]]
	[[Category: Yokoyama, S]]		[[Category: Yokoyama, S]]
	[[Category: Yoneyama, Y]]		[[Category: Yoneyama, Y]]
-	[[Category: Hakuno, F]]
-	[[Category: Takahashi, S]]

OCA at 20:37, 22 December 2016

OCA — Thu, 22 Dec 2016 20:37:58 GMT

←Older revision		Revision as of 20:37, 22 December 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5wrk is ON HOLD	+	The entry 5wrk is ON HOLD until Paper Publication

-	Authors: Yoneyama, Y., Niwa, H., Umehara, T., Yokoyama, S, Hakuno, F., Takahashi, S.	+	Authors: Yoneyama, Y., Niwa, H., Umehara, T., Yokoyama, S., Hakuno, F., Takahashi, S.

	Description: protein in complex with peptide (Y608)		Description: protein in complex with peptide (Y608)
Line 9:		Line 9:
	[[Category: Niwa, H]]		[[Category: Niwa, H]]
	[[Category: Umehara, T]]		[[Category: Umehara, T]]
		+	[[Category: Yokoyama, S]]
	[[Category: Yoneyama, Y]]		[[Category: Yoneyama, Y]]
		+	[[Category: Hakuno, F]]
	[[Category: Takahashi, S]]		[[Category: Takahashi, S]]
-	[[Category: Yokoyama, S, Hakuno, F]]

OCA: Protected "5wrk" [edit=sysop:move=sysop]

OCA — Fri, 09 Dec 2016 18:20:02 GMT

Protected "5wrk" [edit=sysop:move=sysop]

←Older revision

Revision as of 18:20, 9 December 2016

OCA: New page: '''Unreleased structure''' The entry 5wrk is ON HOLD Authors: Yoneyama, Y., Niwa, H., Umehara, T., Yokoyama, S, Hakuno, F., Takahashi, S. Description: protein in complex with peptide (...

OCA — Fri, 09 Dec 2016 18:20:00 GMT

New page: '''Unreleased structure''' The entry 5wrk is ON HOLD Authors: Yoneyama, Y., Niwa, H., Umehara, T., Yokoyama, S, Hakuno, F., Takahashi, S. Description: protein in complex with peptide (...

New page

'''Unreleased structure'''

The entry 5wrk is ON HOLD

Authors: Yoneyama, Y., Niwa, H., Umehara, T., Yokoyama, S, Hakuno, F., Takahashi, S.

Description: protein in complex with peptide (Y608)
[[Category: Unreleased Structures]]
[[Category: Niwa, H]]
[[Category: Umehara, T]]
[[Category: Yoneyama, Y]]
[[Category: Takahashi, S]]
[[Category: Yokoyama, S, Hakuno, F]]