7f69

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7f69]] is a 2 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=7F69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F69 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7f69]] is a 2 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=7F69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F69 FirstGlance]. <br>
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</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=7f69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f69 OCA], [https://pdbe.org/7f69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f69 RCSB], [https://www.ebi.ac.uk/pdbsum/7f69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f69 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7f69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f69 OCA], [https://pdbe.org/7f69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f69 RCSB], [https://www.ebi.ac.uk/pdbsum/7f69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f69 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/WIPI2_HUMAN WIPI2_HUMAN]] The disease is caused by variants affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/WIPI2_HUMAN WIPI2_HUMAN] The disease is caused by variants affecting the gene represented in this entry.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/WIPI2_HUMAN WIPI2_HUMAN]] Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation (PubMed:20505359, PubMed:28561066). Involved in an early step of the formation of preautophagosomal structures (PubMed:20505359, PubMed:28561066). Binds and is activated by phosphatidylinositol 3-phosphate (PtdIns3P) forming on membranes of the endoplasmic reticulum upon activation of the upstream ULK1 and PI3 kinases (PubMed:28561066). Mediates ER-isolation membranes contacts by interacting with the ULK1:RB1CC1 complex and PtdIns3P (PubMed:28890335). Once activated, WIPI2 recruits at phagophore assembly sites the ATG12-ATG5-ATG16L1 complex that directly controls the elongation of the nascent autophagosomal membrane (PubMed:20505359, PubMed:28561066).<ref>PMID:20505359</ref> <ref>PMID:28561066</ref> <ref>PMID:28890335</ref> <ref>PMID:30968111</ref> Recruits the ATG12-ATG5-ATG16L1 complex to omegasomes and preautophagosomal structures, resulting in ATG8 family proteins lipidation and starvation-induced autophagy. Isoform 4 is also required for autophagic clearance of pathogenic bacteria. Isoform 4 binds the membrane surrounding Salmonella and recruits the ATG12-5-16L1 complex, initiating LC3 conjugation, autophagosomal membrane formation, and engulfment of Salmonella.<ref>PMID:24954904</ref>
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[https://www.uniprot.org/uniprot/WIPI2_HUMAN WIPI2_HUMAN] Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation (PubMed:20505359, PubMed:28561066). Involved in an early step of the formation of preautophagosomal structures (PubMed:20505359, PubMed:28561066). Binds and is activated by phosphatidylinositol 3-phosphate (PtdIns3P) forming on membranes of the endoplasmic reticulum upon activation of the upstream ULK1 and PI3 kinases (PubMed:28561066). Mediates ER-isolation membranes contacts by interacting with the ULK1:RB1CC1 complex and PtdIns3P (PubMed:28890335). Once activated, WIPI2 recruits at phagophore assembly sites the ATG12-ATG5-ATG16L1 complex that directly controls the elongation of the nascent autophagosomal membrane (PubMed:20505359, PubMed:28561066).<ref>PMID:20505359</ref> <ref>PMID:28561066</ref> <ref>PMID:28890335</ref> <ref>PMID:30968111</ref> Recruits the ATG12-ATG5-ATG16L1 complex to omegasomes and preautophagosomal structures, resulting in ATG8 family proteins lipidation and starvation-induced autophagy. Isoform 4 is also required for autophagic clearance of pathogenic bacteria. Isoform 4 binds the membrane surrounding Salmonella and recruits the ATG12-5-16L1 complex, initiating LC3 conjugation, autophagosomal membrane formation, and engulfment of Salmonella.<ref>PMID:24954904</ref>
== References ==
== References ==
<references/>
<references/>

Current revision

Crystal structure of WIPI2b in complex with ATG16L1

PDB ID 7f69

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