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Requirement for p62 acetylation in the aggregation of ubiquitylated proteins under nutrient stress
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Requirement for p62 acetylation in the aggregation of ubiquitylated proteins under nutrient stress
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Journal Article
Requirement for p62 acetylation in the aggregation of ubiquitylated proteins under nutrient stress
2019
Overview
Autophagy receptor p62/SQSTM1 promotes the assembly and removal of ubiquitylated proteins by forming p62 bodies and mediating their encapsulation in autophagosomes. Here we show that under nutrient-deficient conditions, cellular p62 specifically undergoes acetylation, which is required for the formation and subsequent autophagic clearance of p62 bodies. We identify K420 and K435 in the UBA domain as the main acetylation sites, and TIP60 and HDAC6 as the acetyltransferase and deacetylase. Mechanically, acetylation at both K420 and K435 sites enhances p62 binding to ubiquitin by disrupting UBA dimerization, while K435 acetylation also directly increases the UBA-ubiquitin affinity. Furthermore, we show that acetylation of p62 facilitates polyubiquitin chain-induced p62 phase separation. Our results suggest an essential role of p62 acetylation in the selective degradation of ubiquitylated proteins in cells under nutrient stress, by specifically regulating the assembly of p62 bodies.
The autophagy receptor p62 mediates the assembly and removal of ubiquitylated protein aggregates by forming p62 bodies. Here, the authors identify an acetylation-dependent mechanism that regulates formation and autophagic clearance of p62 bodies under nutrient-deficient conditions.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/19
/ 140/131
/ 82/58
/ 82/80
/ 82/83
/ 96/109
/ Assembly
/ Histone Deacetylase 6 - metabolism
/ Humanities and Social Sciences
/ Humans
/ Lysine Acetyltransferase 5 - metabolism
/ Protein Aggregates - physiology
/ Protein Binding - physiology
/ Protein Domains - physiology
/ Protein Multimerization - physiology
/ Proteins
/ Science
