title: Function and molecular mechanism of acetylation in autophagy regulation.
abstract: 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.affiliation: State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing, China.
authors.forename: Cong
authors.initials: C
authors.lastname: Yi
authors.forename: Meisheng
authors.initials: M
authors.lastname: Ma
authors.forename: Leili
authors.initials: L
authors.lastname: Ran
authors.forename: Jingxiang
authors.initials: J
authors.lastname: Zheng
authors.forename: Jingjing
authors.initials: J
authors.lastname: Tong
authors.forename: Jing
authors.initials: J
authors.lastname: Zhu
authors.forename: Chengying
authors.initials: C
authors.lastname: Ma
authors.forename: Yufen
authors.initials: Y
authors.lastname: Sun
authors.forename: Shaojin
authors.initials: S
authors.lastname: Zhang
authors.forename: Wenzhi
authors.initials: W
authors.lastname: Feng
authors.forename: Liyuan
authors.initials: L
authors.lastname: Zhu
authors.forename: Yan
authors.initials: Y
authors.lastname: Le
authors.forename: Xingqi
authors.initials: X
authors.lastname: Gong
authors.forename: Xianghua
authors.initials: X
authors.lastname: Yan
authors.forename: Bing
authors.initials: B
authors.lastname: Hong
authors.forename: Fen-Jun
authors.initials: FJ
authors.lastname: Jiang
authors.forename: Zhiping
authors.initials: Z
authors.lastname: Xie
authors.forename: Di
authors.initials: D
authors.lastname: Miao
authors.forename: Haiteng
authors.initials: H
authors.lastname: Deng
authors.forename: Li
authors.initials: L
authors.lastname: Yu
mesh_terms: D000107:Acetylation; D001343:Autophagy; D000071190:Autophagy-Related Protein 8 Family; D000071183:Autophagy-Related Proteins; D002238:Carbohydrate Epimerases / Q000235:genetics / Q000378:metabolism; D051548:Histone Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D006655:Histone Deacetylases / Q000235:genetics / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D009154:Mutation; D010588:Phagosomes / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D044763:Ubiquitin-Conjugating Enzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: C113757:ATG8 protein, S cerevisiae; D000071190:Autophagy-Related Protein 8 Family; D000071183:Autophagy-Related Proteins; D008869:Microtubule-Associated Proteins; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; C496551:Esa1 protein, S cerevisiae; D051548:Histone Acetyltransferases; D044763:Ubiquitin-Conjugating Enzymes; C071665:RPD3 protein, S cerevisiae; D006655:Histone Deacetylases; D002238:Carbohydrate Epimerases; C022554:L-ribulosephosphate 4-epimerase; C104235:ATG3 protein, S cerevisiae