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| | ==Crystal structure of fission yeast Atg8 complexed with the helical AIM of Hfl1.== | | ==Crystal structure of fission yeast Atg8 complexed with the helical AIM of Hfl1.== |
| - | <StructureSection load='6aaf' size='340' side='right' caption='[[6aaf]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='6aaf' size='340' side='right'caption='[[6aaf]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6aaf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AAF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6aaf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AAF FirstGlance]. <br> |
| - | </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=6aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aaf OCA], [http://pdbe.org/6aaf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aaf RCSB], [http://www.ebi.ac.uk/pdbsum/6aaf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aaf ProSAT]</span></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]] 2.197Å</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=6aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aaf OCA], [https://pdbe.org/6aaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aaf RCSB], [https://www.ebi.ac.uk/pdbsum/6aaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aaf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATG8_SCHPO ATG8_SCHPO]] Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Contributes to the maintenance of cell viability under conditions of nitrogen-depletion. Plays a role in meiosis and sporulation and contributes to oxidative stress resistance (PubMed:17295836, PubMed:19778961, PubMed:20070859).[UniProtKB:P38182]<ref>PMID:17295836</ref> <ref>PMID:19778961</ref> <ref>PMID:20070859</ref> | + | [https://www.uniprot.org/uniprot/ATG8_SCHPO ATG8_SCHPO] Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Contributes to the maintenance of cell viability under conditions of nitrogen-depletion. Plays a role in meiosis and sporulation and contributes to oxidative stress resistance (PubMed:17295836, PubMed:19778961, PubMed:20070859).[UniProtKB:P38182]<ref>PMID:17295836</ref> <ref>PMID:19778961</ref> <ref>PMID:20070859</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6aaf" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6aaf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Autophagy-related protein 3D structures|Autophagy-related protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Noda, N N]] | + | [[Category: Large Structures]] |
| - | [[Category: Yamasaki, A]] | + | [[Category: Schizosaccharomyces pombe 972h-]] |
| - | [[Category: Autophagy]] | + | [[Category: Noda NN]] |
| - | [[Category: Membrane protein]] | + | [[Category: Yamasaki A]] |
| - | [[Category: Vacuole]]
| + | |
| Structural highlights
Function
ATG8_SCHPO Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Contributes to the maintenance of cell viability under conditions of nitrogen-depletion. Plays a role in meiosis and sporulation and contributes to oxidative stress resistance (PubMed:17295836, PubMed:19778961, PubMed:20070859).[UniProtKB:P38182][1] [2] [3]
Publication Abstract from PubMed
The ubiquitin-like protein Atg8, in its lipidated form, plays central roles in autophagy. Yet, remarkably, Atg8 also carries out lipidation-independent functions in non-autophagic processes. How Atg8 performs its moonlighting roles is unclear. Here we report that in the fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae, the lipidation-independent roles of Atg8 in maintaining normal morphology and functions of the vacuole require its interaction with a vacuole membrane protein Hfl1 (homolog of human TMEM184 proteins). Crystal structures revealed that the Atg8-Hfl1 interaction is not mediated by the typical Atg8-family-interacting motif (AIM) that forms an intermolecular beta-sheet with Atg8. Instead, the Atg8-binding regions in Hfl1 proteins adopt a helical conformation, thus representing a new type of AIMs (termed helical AIMs here). These results deepen our understanding of both the functional versatility of Atg8 and the mechanistic diversity of Atg8 binding.
Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein.,Liu XM, Yamasaki A, Du XM, Coffman VC, Ohsumi Y, Nakatogawa H, Wu JQ, Noda NN, Du LL Elife. 2018 Nov 19;7. pii: 41237. doi: 10.7554/eLife.41237. PMID:30451685[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kohda TA, Tanaka K, Konomi M, Sato M, Osumi M, Yamamoto M. Fission yeast autophagy induced by nitrogen starvation generates a nitrogen source that drives adaptation processes. Genes Cells. 2007 Feb;12(2):155-70. PMID:17295836 doi:http://dx.doi.org/10.1111/j.1365-2443.2007.01041.x
- ↑ Mukaiyama H, Kajiwara S, Hosomi A, Giga-Hama Y, Tanaka N, Nakamura T, Takegawa K. Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial sporulation during nitrogen starvation. Microbiology. 2009 Dec;155(Pt 12):3816-26. Epub 2009 Sep 24. PMID:19778961 doi:http://dx.doi.org/mic.0.034389-0
- ↑ Mikawa T, Kanoh J, Ishikawa F. Fission yeast Vps1 and Atg8 contribute to oxidative stress resistance. Genes Cells. 2010 Jan 13. PMID:20070859 doi:http://dx.doi.org/GTC1376
- ↑ Liu XM, Yamasaki A, Du XM, Coffman VC, Ohsumi Y, Nakatogawa H, Wu JQ, Noda NN, Du LL. Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein. Elife. 2018 Nov 19;7. pii: 41237. doi: 10.7554/eLife.41237. PMID:30451685 doi:http://dx.doi.org/10.7554/eLife.41237
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