4uqi - Revision history

OCA at 10:33, 10 January 2024

OCA — Wed, 10 Jan 2024 10:33:02 GMT

←Older revision		Revision as of 10:33, 10 January 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UQI FirstGlance]. <br>		<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UQI FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</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]] 2.79Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [https://pdbe.org/4uqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [https://www.ebi.ac.uk/pdbsum/4uqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqi 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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [https://pdbe.org/4uqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [https://www.ebi.ac.uk/pdbsum/4uqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqi ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:32, 29 March 2023

OCA — Wed, 29 Mar 2023 07:32:40 GMT

←Older revision		Revision as of 07:32, 29 March 2023
Line 3:		Line 3:
	<StructureSection load='4uqi' size='340' side='right'caption='[[4uqi]], [[Resolution\|resolution]] 2.79Å' scene=''>		<StructureSection load='4uqi' size='340' side='right'caption='[[4uqi]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~], [~~http~~://en.wikipedia.org/wiki/~~Human Human~~] and [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=4UQI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UQI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [~~http~~://pdbe.org/4uqi PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4uqi PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqi 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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [https://pdbe.org/4uqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [https://www.ebi.ac.uk/pdbsum/4uqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqi ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/AP2S1_MOUSE AP2S1_MOUSE]] 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 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity).<ref>PMID:14745134</ref> <ref>PMID:15473838</ref> [[http://www.uniprot.org/uniprot/AP2A2_RAT AP2A2_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 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity).<ref>PMID:14745134</ref> <ref>PMID:15473838</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/AP2B1_HUMAN AP2B1_HUMAN]] 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 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly.<ref>PMID:14745134</ref> <ref>PMID:15473838</ref> <ref>PMID:14985334</ref> <ref>PMID:19033387</ref>	+	[https://www.uniprot.org/uniprot/AP2A2_RAT AP2A2_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 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity).<ref>PMID:14745134</ref> <ref>PMID:15473838</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buffalo rat]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Dannhauser~~, P N~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Graham~~, S C~~]]	+	[[Category: Dannhauser PN]]
-	[[Category: Hoening, S]]	+	[[Category: Graham SC]]
-	[[Category: Kelly~~, B T~~]]	+	[[Category: Hoening S]]
-	[[Category: Liska, N]]	+	[[Category: Kelly BT]]
-	[[Category: Owen~~, D J~~]]	+	[[Category: Liska N]]
-	[[Category: Ungewickell~~, E J]]~~	+	[[Category: Owen DJ]]
-	~~[[Category: Endocytosis]]~~	+	[[Category: Ungewickell EJ]]
-	~~[[Category: Lipid binding]]~~	+
-	~~[[Category: Protein transport~~]]	+

OCA at 06:24, 7 October 2020

OCA — Wed, 07 Oct 2020 06:24:46 GMT

←Older revision		Revision as of 06:24, 7 October 2020
Line 3:		Line 3:
	<StructureSection load='4uqi' size='340' side='right'caption='[[4uqi]], [[Resolution\|resolution]] 2.79Å' scene=''>		<StructureSection load='4uqi' size='340' side='right'caption='[[4uqi]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat], [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4UQI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat], [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4UQI FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://pdbe.org/4uqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqi 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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://pdbe.org/4uqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqi ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 09:21, 21 May 2019

OCA — Tue, 21 May 2019 09:21:24 GMT

←Older revision		Revision as of 09:21, 21 May 2019
Line 1:		Line 1:

	==AP2 controls clathrin polymerization with a membrane-activated switch==		==AP2 controls clathrin polymerization with a membrane-activated switch==
-	<StructureSection load='4uqi' size='340' side='right' caption='[[4uqi]], [[Resolution\|resolution]] 2.79Å' scene=''>	+	<StructureSection load='4uqi' size='340' side='right'caption='[[4uqi]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UQI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat], [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UQI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://pdbe.org/4uqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqi 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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://pdbe.org/4uqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqi ProSAT]</span></td></tr>
Line 20:		Line 20:

	==See Also==		==See Also==
-	*[[Adaptin\|Adaptin]]	+	*[[Adaptin 3D structures\|Adaptin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
		+	[[Category: Lk3 transgenic mice]]
	[[Category: Dannhauser, P N]]		[[Category: Dannhauser, P N]]
	[[Category: Graham, S C]]		[[Category: Graham, S C]]

OCA at 14:21, 4 August 2016

OCA — Thu, 04 Aug 2016 14:21:14 GMT

←Older revision		Revision as of 14:21, 4 August 2016
Line 1:		Line 1:
		+
	==AP2 controls clathrin polymerization with a membrane-activated switch==		==AP2 controls clathrin polymerization with a membrane-activated switch==
	<StructureSection load='4uqi' size='340' side='right' caption='[[4uqi]], [[Resolution\|resolution]] 2.79Å' scene=''>		<StructureSection load='4uqi' size='340' side='right' caption='[[4uqi]], [[Resolution\|resolution]] 2.79Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UQI FirstGlance]. <br>		<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UQI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi 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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://pdbe.org/4uqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqi 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 4uqi" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Adaptin\|Adaptin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:39, 24 December 2014

OCA — Wed, 24 Dec 2014 15:39:09 GMT

←Older revision		Revision as of 15:39, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UQI FirstGlance]. <br>		<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UQI FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi 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=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AP2S1_MOUSE AP2S1_MOUSE]] 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 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity).<ref>PMID:14745134</ref> <ref>PMID:15473838</ref> [[http://www.uniprot.org/uniprot/AP2A2_RAT AP2A2_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 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity).<ref>PMID:14745134</ref> <ref>PMID:15473838</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/AP2B1_HUMAN AP2B1_HUMAN]] 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 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly.<ref>PMID:14745134</ref> <ref>PMID:15473838</ref> <ref>PMID:14985334</ref> <ref>PMID:19033387</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 20:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Dannhauser, P N.]]	+	[[Category: Dannhauser, P N]]
-	[[Category: Graham, S C.]]	+	[[Category: Graham, S C]]
-	[[Category: Hoening, S.]]	+	[[Category: Hoening, S]]
-	[[Category: Kelly, B T.]]	+	[[Category: Kelly, B T]]
-	[[Category: Liska, N.]]	+	[[Category: Liska, N]]
-	[[Category: Owen, D J.]]	+	[[Category: Owen, D J]]
-	[[Category: Ungewickell, E J.]]	+	[[Category: Ungewickell, E J]]
	[[Category: Endocytosis]]		[[Category: Endocytosis]]
	[[Category: Lipid binding]]		[[Category: Lipid binding]]
	[[Category: Protein transport]]		[[Category: Protein transport]]

OCA at 02:26, 7 August 2014

OCA — Thu, 07 Aug 2014 02:26:06 GMT

←Older revision		Revision as of 02:26, 7 August 2014
Line 6:		Line 6:
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi PDBsum]</span></td></tr>		<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi PDBsum]</span></td></tr>
	<table>		<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Clathrin-mediated endocytosis (CME) is vital for the internalization of most cell-surface proteins. In CME, plasma membrane-binding clathrin adaptors recruit and polymerize clathrin to form clathrin-coated pits into which cargo is sorted. Assembly polypeptide 2 (AP2) is the most abundant adaptor and is pivotal to CME. Here, we determined a structure of AP2 that includes the clathrin-binding beta2 hinge and developed an AP2-dependent budding assay. Our findings suggest that an autoinhibitory mechanism prevents clathrin recruitment by cytosolic AP2. A large-scale conformational change driven by the plasma membrane phosphoinositide phosphatidylinositol 4,5-bisphosphate and cargo relieves this autoinhibition, triggering clathrin recruitment and hence clathrin-coated bud formation. This molecular switching mechanism can couple AP2's membrane recruitment to its key functions of cargo and clathrin binding.
		+
		+	Clathrin adaptors. AP2 controls clathrin polymerization with a membrane-activated switch.,Kelly BT, Graham SC, Liska N, Dannhauser PN, Honing S, Ungewickell EJ, Owen DJ Science. 2014 Jul 25;345(6195):459-63. doi: 10.1126/science.1254836. PMID:25061211<ref>PMID:25061211</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:56, 30 July 2014

OCA — Wed, 30 Jul 2014 07:56:39 GMT

←Older revision		Revision as of 07:56, 30 July 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==AP2 controls clathrin polymerization with a membrane-activated switch==
-		+	<StructureSection load='4uqi' size='340' side='right' caption='[[4uqi]], [[Resolution\|resolution]] 2.79Å' scene=''>
-	~~The entry~~ 4uqi is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4uqi]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UQI FirstGlance]. <br>
-	~~Authors~~: ~~Kelly~~, B.T., ~~Graham, S~~.C., ~~Liska, N~~., Dannhauser, P.N., Hoening, S., ~~Ungewickell, E.J~~., Owen, D.J.	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene><br>
-		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqi RCSB], [http://www.ebi.ac.uk/pdbsum/4uqi PDBsum]</span></td></tr>
-	~~Description~~: ~~AP2 controls clathrin polymerization with a membrane-activated switch~~	+	<table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Dannhauser, P N.]]
		+	[[Category: Graham, S C.]]
		+	[[Category: Hoening, S.]]
		+	[[Category: Kelly, B T.]]
		+	[[Category: Liska, N.]]
		+	[[Category: Owen, D J.]]
		+	[[Category: Ungewickell, E J.]]
		+	[[Category: Endocytosis]]
		+	[[Category: Lipid binding]]
		+	[[Category: Protein transport]]

OCA: Protected "4uqi" [edit=sysop:move=sysop]

OCA — Wed, 02 Jul 2014 07:37:51 GMT

Protected "4uqi" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:37, 2 July 2014

OCA: New page: '''Unreleased structure''' The entry 4uqi is ON HOLD until Paper Publication Authors: Kelly, B.T., Graham, S.C., Liska, N., Dannhauser, P.N., Hoening, S., Ungewickell, E.J., Owen, D.J. ...

OCA — Wed, 02 Jul 2014 07:37:50 GMT

New page: '''Unreleased structure''' The entry 4uqi is ON HOLD until Paper Publication Authors: Kelly, B.T., Graham, S.C., Liska, N., Dannhauser, P.N., Hoening, S., Ungewickell, E.J., Owen, D.J. ...

New page

'''Unreleased structure'''

The entry 4uqi is ON HOLD until Paper Publication

Authors: Kelly, B.T., Graham, S.C., Liska, N., Dannhauser, P.N., Hoening, S., Ungewickell, E.J., Owen, D.J.

Description: AP2 controls clathrin polymerization with a membrane-activated switch