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| | <StructureSection load='5jge' size='340' side='right'caption='[[5jge]], [[Resolution|resolution]] 1.91Å' scene=''> | | <StructureSection load='5jge' size='340' side='right'caption='[[5jge]], [[Resolution|resolution]] 1.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jge]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JGE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JGE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jge]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JGE FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jgf|5jgf]]</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]] 1.91Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATG19, CVT19, YOL082W, O0980, YOL01 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=5jge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jge OCA], [https://pdbe.org/5jge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jge RCSB], [https://www.ebi.ac.uk/pdbsum/5jge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jge ProSAT]</span></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=5jge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jge OCA], [http://pdbe.org/5jge PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jge RCSB], [http://www.ebi.ac.uk/pdbsum/5jge PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jge ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATG19_YEAST ATG19_YEAST]] Cargo-receptor protein involved in the cytoplasm to vacuole transport (Cvt) and in autophagy. Recognizes cargo proteins, such as APE4, LAP3, LAP4 and AMS1 and delivers them to the pre-autophagosomal structure for eventual engulfment by the autophagosome and targeting to the vacuole. Involved in the organization of the preautophagosomal structure (PAS). ATG19 association with cargo protein is required to localize ATG11 to the PAS. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates, and is essential for the survival of cells subjected to severe ER stress. Plays also a role in regulation of filamentous growth.<ref>PMID:11382752</ref> <ref>PMID:11430817</ref> <ref>PMID:12479807</ref> <ref>PMID:12479808</ref> <ref>PMID:15138258</ref> <ref>PMID:15801807</ref> <ref>PMID:16186126</ref> <ref>PMID:15659643</ref> <ref>PMID:17132049</ref> <ref>PMID:17700056</ref> <ref>PMID:17192412</ref> <ref>PMID:17238920</ref> <ref>PMID:19061865</ref> <ref>PMID:21228276</ref> <ref>PMID:19021777</ref> <ref>PMID:20659891</ref> | + | [https://www.uniprot.org/uniprot/ATG19_YEAST ATG19_YEAST] Cargo-receptor protein involved in the cytoplasm to vacuole transport (Cvt) and in autophagy. Recognizes cargo proteins, such as APE4, LAP3, LAP4 and AMS1 and delivers them to the pre-autophagosomal structure for eventual engulfment by the autophagosome and targeting to the vacuole. Involved in the organization of the preautophagosomal structure (PAS). ATG19 association with cargo protein is required to localize ATG11 to the PAS. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates, and is essential for the survival of cells subjected to severe ER stress. Plays also a role in regulation of filamentous growth.<ref>PMID:11382752</ref> <ref>PMID:11430817</ref> <ref>PMID:12479807</ref> <ref>PMID:12479808</ref> <ref>PMID:15138258</ref> <ref>PMID:15801807</ref> <ref>PMID:16186126</ref> <ref>PMID:15659643</ref> <ref>PMID:17132049</ref> <ref>PMID:17700056</ref> <ref>PMID:17192412</ref> <ref>PMID:17238920</ref> <ref>PMID:19061865</ref> <ref>PMID:21228276</ref> <ref>PMID:19021777</ref> <ref>PMID:20659891</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Selective autophagy mediates the degradation of various cargoes, including protein aggregates and organelles, thereby contributing to cellular homeostasis. Cargo receptors ensure selectivity by tethering specific cargo to lipidated Atg8 at the isolation membrane. However, little is known about the structural requirements underlying receptor-mediated cargo recognition. Here, we report structural, biochemical, and cell biological analysis of the major selective cargo protein in budding yeast, aminopeptidase I (Ape1), and its complex with the receptor Atg19. The Ape1 propeptide has a trimeric coiled-coil structure, which tethers dodecameric Ape1 bodies together to form large aggregates. Atg19 disassembles the propeptide trimer and forms a 2:1 heterotrimer, which not only blankets the Ape1 aggregates but also regulates their size. These receptor activities may promote elongation of the isolation membrane along the aggregate surface, enabling sequestration of the cargo with high specificity.
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| - | | + | |
| - | Structural Basis for Receptor-Mediated Selective Autophagy of Aminopeptidase I Aggregates.,Yamasaki A, Watanabe Y, Adachi W, Suzuki K, Matoba K, Kirisako H, Kumeta H, Nakatogawa H, Ohsumi Y, Inagaki F, Noda NN Cell Rep. 2016 Jun 28;16(1):19-27. doi: 10.1016/j.celrep.2016.05.066. Epub 2016, Jun 16. PMID:27320913<ref>PMID:27320913</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5jge" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Noda, N N]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Watanabe, Y]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Complex]] | + | [[Category: Noda NN]] |
| - | [[Category: Protein transport]] | + | [[Category: Watanabe Y]] |
| - | [[Category: Receptor]]
| + | |
| Structural highlights
Function
ATG19_YEAST Cargo-receptor protein involved in the cytoplasm to vacuole transport (Cvt) and in autophagy. Recognizes cargo proteins, such as APE4, LAP3, LAP4 and AMS1 and delivers them to the pre-autophagosomal structure for eventual engulfment by the autophagosome and targeting to the vacuole. Involved in the organization of the preautophagosomal structure (PAS). ATG19 association with cargo protein is required to localize ATG11 to the PAS. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates, and is essential for the survival of cells subjected to severe ER stress. Plays also a role in regulation of filamentous growth.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16]
References
- ↑ Leber R, Silles E, Sandoval IV, Mazon MJ. Yol082p, a novel CVT protein involved in the selective targeting of aminopeptidase I to the yeast vacuole. J Biol Chem. 2001 Aug 3;276(31):29210-7. Epub 2001 May 29. PMID:11382752 doi:http://dx.doi.org/10.1074/jbc.M101438200
- ↑ Scott SV, Guan J, Hutchins MU, Kim J, Klionsky DJ. Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway. Mol Cell. 2001 Jun;7(6):1131-41. PMID:11430817
- ↑ Suzuki K, Kamada Y, Ohsumi Y. Studies of cargo delivery to the vacuole mediated by autophagosomes in Saccharomyces cerevisiae. Dev Cell. 2002 Dec;3(6):815-24. PMID:12479807
- ↑ Shintani T, Huang WP, Stromhaug PE, Klionsky DJ. Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway. Dev Cell. 2002 Dec;3(6):825-37. PMID:12479808
- ↑ Shintani T, Klionsky DJ. Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway. J Biol Chem. 2004 Jul 16;279(29):29889-94. Epub 2004 May 11. PMID:15138258 doi:http://dx.doi.org/10.1074/jbc.M404399200
- ↑ Cebollero E, Carrascosa AV, Gonzalez R. Evidence for yeast autophagy during simulation of sparkling wine aging: a reappraisal of the mechanism of yeast autolysis in wine. Biotechnol Prog. 2005 Mar-Apr;21(2):614-6. PMID:15801807 doi:http://dx.doi.org/10.1021/bp049708y
- ↑ Baxter BK, Abeliovich H, Zhang X, Stirling AG, Burlingame AL, Goldfarb DS. Atg19p ubiquitination and the cytoplasm to vacuole trafficking pathway in yeast. J Biol Chem. 2005 Nov 25;280(47):39067-76. Epub 2005 Sep 26. PMID:16186126 doi:http://dx.doi.org/10.1074/jbc.M508064200
- ↑ Yorimitsu T, Klionsky DJ. Atg11 links cargo to the vesicle-forming machinery in the cytoplasm to vacuole targeting pathway. Mol Biol Cell. 2005 Apr;16(4):1593-605. Epub 2005 Jan 19. PMID:15659643 doi:http://dx.doi.org/10.1091/mbc.E04-11-1035
- ↑ Bernales S, McDonald KL, Walter P. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol. 2006 Nov;4(12):e423. PMID:17132049 doi:http://dx.doi.org/10.1371/journal.pbio.0040423
- ↑ Ma J, Jin R, Dobry CJ, Lawson SK, Kumar A. Overexpression of autophagy-related genes inhibits yeast filamentous growth. Autophagy. 2007 Nov-Dec;3(6):604-9. Epub 2007 Jul 24. PMID:17700056
- ↑ Chang CY, Huang WP. Atg19 mediates a dual interaction cargo sorting mechanism in selective autophagy. Mol Biol Cell. 2007 Mar;18(3):919-29. Epub 2006 Dec 27. PMID:17192412 doi:http://dx.doi.org/10.1091/mbc.E06-08-0683
- ↑ Mazon MJ, Eraso P, Portillo F. Efficient degradation of misfolded mutant Pma1 by endoplasmic reticulum-associated degradation requires Atg19 and the Cvt/autophagy pathway. Mol Microbiol. 2007 Feb;63(4):1069-77. PMID:17238920 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05580.x
- ↑ Kageyama T, Suzuki K, Ohsumi Y. Lap3 is a selective target of autophagy in yeast, Saccharomyces cerevisiae. Biochem Biophys Res Commun. 2009 Jan 16;378(3):551-7. doi:, 10.1016/j.bbrc.2008.11.084. Epub 2008 Dec 4. PMID:19061865 doi:http://dx.doi.org/10.1016/j.bbrc.2008.11.084
- ↑ Kario E, Amar N, Elazar Z, Navon A. A new autophagy-related checkpoint in the degradation of an ERAD-M target. J Biol Chem. 2011 Apr 1;286(13):11479-91. doi: 10.1074/jbc.M110.177618. Epub 2011, Jan 12. PMID:21228276 doi:http://dx.doi.org/10.1074/jbc.M110.177618
- ↑ Noda NN, Kumeta H, Nakatogawa H, Satoo K, Adachi W, Ishii J, Fujioka Y, Ohsumi Y, Inagaki F. Structural basis of target recognition by Atg8/LC3 during selective autophagy. Genes Cells. 2008 Oct 22. PMID:19021777 doi:GTC1238
- ↑ Watanabe Y, Noda NN, Kumeta H, Suzuki K, Ohsumi Y, Inagaki F. Selective transport of alpha-mannosidase by autophagic pathways: structural basis for cargo recognition by Atg19 and Atg34. J Biol Chem. 2010 Sep 24;285(39):30026-33. Epub 2010 Jul 21. PMID:20659891 doi:http://dx.doi.org/10.1074/jbc.M110.143545
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