| Physiological pH and acidic phospholipids contribute to substrate specificity in lipidation of Atg8. | |
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MedLine Citation:
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PMID: 18544538 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Yeast Atg8 and its mammalian homolog LC3 are ubiquitin-like proteins involved in autophagy, a primary pathway for degradation of cytosolic constituents in vacuoles/lysosomes. Whereas the lipid phosphatidylethanolamine (PE) was identified as the sole in vivo target of their conjugation reactions, in vitro studies showed that the same system can mediate the conjugation of these proteins with phosphatidylserine as efficiently as with PE. Here, we show that, in contrast to PE conjugation, the in vitro phosphatidylserine conjugation of Atg8 is markedly suppressed at physiological pH. Furthermore, the addition of acidic phospholipids to liposomes also results in the preferential formation of the Atg8-PE conjugate. We have successfully captured authentic thioester intermediates, allowing us to elucidate which step in the conjugation reaction is affected by these changes in pH and membrane lipid composition. We propose that these factors contribute to the selective formation of Atg8-PE in the cell. |
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Authors:
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Kyoko Oh-oka; Hitoshi Nakatogawa; Yoshinori Ohsumi |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-06-10 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 283 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2008 Aug |
Date Detail:
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Created Date: 2008-08-04 Completed Date: 2008-09-17 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 21847-52 Citation Subset: IM |
Affiliation:
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Department of Cell Biology, National Institute for Basic Biology, Graduate University for Advanced Studies, Okazaki 444-8585, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Hydrogen-Ion Concentration Liposomes / metabolism Microtubule-Associated Proteins / metabolism* Phosphatidylethanolamines / metabolism Phosphatidylserines / metabolism Phospholipids / metabolism* Saccharomyces cerevisiae / metabolism* Saccharomyces cerevisiae Proteins / metabolism* Substrate Specificity Time Factors Ubiquitin-Conjugating Enzymes |
| Chemical | |
Reg. No./Substance:
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0/ATG3 protein, S cerevisiae; 0/ATG8 protein, S cerevisiae; 0/Liposomes; 0/Microtubule-Associated Proteins; 0/Phosphatidylethanolamines; 0/Phosphatidylserines; 0/Phospholipids; 0/Saccharomyces cerevisiae Proteins; 39382-08-6/phosphatidylethanolamine; EC 6.3.2.19/Ubiquitin-Conjugating Enzymes |
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