8afx
From Proteopedia
(Difference between revisions)
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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=8afx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8afx OCA], [https://pdbe.org/8afx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8afx RCSB], [https://www.ebi.ac.uk/pdbsum/8afx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8afx 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=8afx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8afx OCA], [https://pdbe.org/8afx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8afx RCSB], [https://www.ebi.ac.uk/pdbsum/8afx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8afx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ATG18_YEAST ATG18_YEAST] The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). May negatively regulate FAB1 activity by sequestering or masking VAC7 from FAB1. Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation-induced autophagy. Involved in correct ATG9 trafficking to the pre-autophagosomal structure. Might also be involved in premeiotic DNA replication. With ATG2, protects ATG8 from ATG4-mediated cleavage.<ref>PMID:11470404</ref> <ref>PMID:11536337</ref> <ref>PMID:11707261</ref> <ref>PMID:11739783</ref> <ref>PMID:14723849</ref> <ref>PMID:15155809</ref> <ref>PMID:15194695</ref> <ref>PMID:16876790</ref> <ref>PMID:17699591</ref> <ref>PMID:18586673</ref> <ref>PMID:18769150</ref> <ref>PMID:19037259</ref> <ref>PMID:20154084</ref> <ref>PMID:22108003</ref> <ref>PMID:22728243</ref> <ref>PMID:22787281</ref> <ref>PMID:24905091</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Autophagy-related protein 18 (Atg18) participates in the elongation of early autophagosomal structures in concert with Atg2 and Atg9 complexes. How Atg18 contributes to the structural coordination of Atg2 and Atg9 at the isolation membrane remains to be understood. Here, we determined the cryo-EM structures of Atg18 organized in helical tubes, Atg18 oligomers in solution as well as on lipid membrane scaffolds. The helical assembly is composed of Atg18 tetramers forming a lozenge cylindrical lattice with remarkable structural similarity to the COPII outer coat. When reconstituted with lipid membranes, using subtomogram averaging we determined tilted Atg18 dimer structures bridging two juxtaposed lipid membranes spaced apart by 80 A. Moreover, lipid reconstitution experiments further delineate the contributions of Atg18's FRRG motif and the amphipathic helical extension in membrane interaction. The observed structural plasticity of Atg18's oligomeric organization and membrane binding properties provide a molecular framework for the positioning of downstream components of the autophagy machinery. | ||
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| + | Atg18 oligomer organization in assembled tubes and on lipid membrane scaffolds.,Mann D, Fromm SA, Martinez-Sanchez A, Gopaldass N, Choy R, Mayer A, Sachse C Nat Commun. 2023 Dec 6;14(1):8086. doi: 10.1038/s41467-023-43460-3. PMID:38057304<ref>PMID:38057304</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8afx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Single particle structure of Atg18-WT
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