Phosphorylation of Atg31 is required for autophagy

Protein & Cell
Wenzhi FengLi Yu

Abstract

Autophagy is an evolutionarily conserved cellular process which degrades intracellular contents. The Atg17-Atg31-Atg29 complex plays a key role in autophagy induction by various stimuli. In yeast, autophagy occurs with autophagosome formation at a special site near the vacuole named the pre-autophagosomal structure (PAS). The Atg17-Atg31-Atg29 complex forms a scaffold for PAS organization, and recruits other autophagy-related (Atg) proteins to the PAS. Here, we show that Atg31 is a phosphorylated protein. The phosphorylation sites on Atg31 were identified by mass spectrometry. Analysis of mutants in which the phosphorylated amino acids were replaced by alanine, either individually or in various combinations, identified S174 as the functional phosphorylation site. An S174A mutant showed a similar degree of autophagy impairment as an Atg31 deletion mutant. S174 phosphorylation is required for autophagy induced by various autophagy stimuli such as nitrogen starvation and rapamycin treatment. Mass spectrometry analysis showed that S174 is phosphorylated constitutively, and expression of a phosphorylation-mimic mutant (S174D) in the Atg31 deletion strain restores autophagy. In the S174A mutant, Atg9-positive vesicles accumulate at t...Continue Reading

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Citations

Feb 26, 2016·Journal of Molecular Biology·Xin Wen, Daniel J Klionsky
Nov 15, 2015·Journal of Cell Science·Jing ZhuZhiping Xie
Jan 29, 2020·Developmental Cell·Fei WangSoni Lacefield
May 11, 2021·Autophagy·Mariya LichevaFulvio Reggiori

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Methods Mentioned

BETA
two-hybrid
confocal microscopy
PCR

Software Mentioned

Proteome Discoverer
Xcalibur
IUPred
ANCHOR
Modeller
FIT
TASSER
Pondr
Pymol
IUPed

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