Journal
SCIENCE
Volume 336, Issue 6080, Pages 474-477Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1216990
Keywords
-
Categories
Funding
- 973 Program [2011CB910101, 2010CB833704]
- National Science Foundation [31030043, 31125018, 30971484, 30971441, 31172290, 31072036]
- Tsinghua University [2010THZ0, 2009THZ03071]
Ask authors/readers for more resources
Protein acetylation emerged as a key regulatory mechanism for many cellular processes. We used genetic analysis of Saccharomyces 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 Atg8. 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available