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| | <StructureSection load='6rgo' size='340' side='right'caption='[[6rgo]], [[Resolution|resolution]] 3.70Å' scene=''> | | <StructureSection load='6rgo' size='340' side='right'caption='[[6rgo]], [[Resolution|resolution]] 3.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rgo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ashgo Ashgo] and [http://en.wikipedia.org/wiki/Candida_sphaerica Candida sphaerica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RGO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RGO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rgo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eremothecium_gossypii_ATCC_10895 Eremothecium gossypii ATCC 10895] and [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RGO FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATG21, KLLA0E24354g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284590 Candida sphaerica]), ATG16, AFL186W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284811 ASHGO])</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]] 3.701Å</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=6rgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rgo OCA], [http://pdbe.org/6rgo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rgo RCSB], [http://www.ebi.ac.uk/pdbsum/6rgo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rgo 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=6rgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rgo OCA], [https://pdbe.org/6rgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rgo RCSB], [https://www.ebi.ac.uk/pdbsum/6rgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rgo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATG21_KLULA ATG21_KLULA]] Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity). [[http://www.uniprot.org/uniprot/ATG16_ASHGO ATG16_ASHGO]] Stabilizes the ATG5-ATG12 conjugate which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity). | + | [https://www.uniprot.org/uniprot/ATG21_KLULA ATG21_KLULA] Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ashgo]] | + | [[Category: Eremothecium gossypii ATCC 10895]] |
| - | [[Category: Candida sphaerica]] | + | [[Category: Kluyveromyces lactis NRRL Y-1140]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Neumann, P]] | + | [[Category: Neumann P]] |
| - | [[Category: Thumm, M]] | + | [[Category: Thumm M]] |
| - | [[Category: Atg16]]
| + | |
| - | [[Category: Atg21]]
| + | |
| - | [[Category: Atg8 lipidation]]
| + | |
| - | [[Category: Autophagy]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Yeast]]
| + | |
| Structural highlights
Function
ATG21_KLULA Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity).
Publication Abstract from PubMed
Coupling of Atg8 to phosphatidylethanolamine is crucial for the expansion of the crescent-shaped phagophore during cargo engulfment. Atg21, a PtdIns3P-binding beta-propeller protein, scaffolds Atg8 and its E3-like complex Atg12-Atg5-Atg16 during lipidation. The crystal structure of Atg21, in complex with the Atg16 coiled-coil domain, showed its binding at the bottom side of the Atg21 beta-propeller. Our structure allowed detailed analyses of the complex formation of Atg21 with Atg16 and uncovered the orientation of the Atg16 coiled-coil domain with respect to the membrane. We further found that Atg21 was restricted to the phagophore edge, near the vacuole, known as the vacuole isolation membrane contact site (VICS). We identified a specialized vacuolar subdomain at the VICS, typical of organellar contact sites, where the membrane protein Vph1 was excluded, while Vac8 was concentrated. Furthermore, Vac8 was required for VICS formation. Our results support a specialized organellar contact involved in controlling phagophore elongation.
Atg21 organizes Atg8 lipidation at the contact of the vacuole with the phagophore.,Munzel L, Neumann P, Otto FB, Krick R, Metje-Sprink J, Kroppen B, Karedla N, Enderlein J, Meinecke M, Ficner R, Thumm M Autophagy. 2020 Jun 9:1-21. doi: 10.1080/15548627.2020.1766332. PMID:32515645[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Munzel L, Neumann P, Otto FB, Krick R, Metje-Sprink J, Kroppen B, Karedla N, Enderlein J, Meinecke M, Ficner R, Thumm M. Atg21 organizes Atg8 lipidation at the contact of the vacuole with the phagophore. Autophagy. 2020 Jun 9:1-21. doi: 10.1080/15548627.2020.1766332. PMID:32515645 doi:http://dx.doi.org/10.1080/15548627.2020.1766332
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