8afz
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8afz]] is a 3 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=8AFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AFZ FirstGlance]. <br> | <table><tr><td colspan='2'>[[8afz]] is a 3 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=8AFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AFZ FirstGlance]. <br> | ||
| - | </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=8afz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8afz OCA], [https://pdbe.org/8afz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8afz RCSB], [https://www.ebi.ac.uk/pdbsum/8afz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8afz ProSAT]</span></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]] 10Å</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=8afz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8afz OCA], [https://pdbe.org/8afz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8afz RCSB], [https://www.ebi.ac.uk/pdbsum/8afz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8afz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SNX1_HUMAN SNX1_HUMAN] May be involved in several stages of intracellular trafficking. Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).<ref>PMID:12198132</ref> <ref>PMID:15498486</ref> <ref>PMID:17101778</ref> | [https://www.uniprot.org/uniprot/SNX1_HUMAN SNX1_HUMAN] May be involved in several stages of intracellular trafficking. Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).<ref>PMID:12198132</ref> <ref>PMID:15498486</ref> <ref>PMID:17101778</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Recycling of membrane proteins enables the reuse of receptors, ion channels and transporters. A key component of the recycling machinery is the endosomal sorting complex for promoting exit 1 (ESCPE-1), which rescues transmembrane proteins from the endolysosomal pathway for transport to the trans-Golgi network and the plasma membrane. This rescue entails the formation of recycling tubules through ESCPE-1 recruitment, cargo capture, coat assembly and membrane sculpting by mechanisms that remain largely unknown. Herein, we show that ESCPE-1 has a single-layer coat organization and suggest how synergistic interactions between ESCPE-1 protomers, phosphoinositides and cargo molecules result in a global arrangement of amphipathic helices to drive tubule formation. Our results thus define a key process of tubule-based endosomal sorting. | ||
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| + | Architecture of the ESCPE-1 membrane coat.,Lopez-Robles C, Scaramuzza S, Astorga-Simon EN, Ishida M, Williamson CD, Banos-Mateos S, Gil-Carton D, Romero-Durana M, Vidaurrazaga A, Fernandez-Recio J, Rojas AL, Bonifacino JS, Castano-Diez D, Hierro A Nat Struct Mol Biol. 2023 Jul;30(7):958-969. doi: 10.1038/s41594-023-01014-7. , Epub 2023 Jun 15. PMID:37322239<ref>PMID:37322239</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8afz" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Sorting nexin 3D structures|Sorting nexin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Architecture of the ESCPE-1 membrane coat
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