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Function and Molecular Mechanism of Acetylation in Autophagy Regulation.
- Source :
-
Science . 4/27/2012, Vol. 336 Issue 6080, p474-477. 4p. - Publication Year :
- 2012
-
Abstract
- Protein acetylation emerged as a key regulatory mechanism for many cellular processes. We used genetic analysis of Saccharornyces cerevisiae to identify Esa1 as a histone acetyltransferase required for autophagy. We further identified the autophagy signaling component Atg3 as a substrate for Esa1. Specifically, acetylation of K19 and K48 of Atg3 regulated autophagy by controlling Atg3 and Atg8 interaction and lipidation of AtgS. Starvation induced transient K19-K48 acetylation through spatial and temporal regulation of the localization of acetylase Esa1 and the deacetylase Rpd3 on pre-autophagosomal structures (PASs) and their interaction with Atg3. Attenuation of K19-K48 acetylation was associated with attenuation of autophagy. Increased K19-K48 acetylation after deletion of the deacetylase Rpd3 caused increased autophagy. Thus, protein acetylation contributes to control of autophagy. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00368075
- Volume :
- 336
- Issue :
- 6080
- Database :
- Academic Search Index
- Journal :
- Science
- Publication Type :
- Academic Journal
- Accession number :
- 75246086
- Full Text :
- https://doi.org/10.1126/science.1216990