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2015 ; 6
(4
): 288-96
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Phosphorylation of Atg31 is required for autophagy
#MMPMID25773276
Feng W
; Wu T
; Dan X
; Chen Y
; Li L
; Chen S
; Miao D
; Deng H
; Gong X
; Yu L
Protein Cell
2015[Apr]; 6
(4
): 288-96
PMID25773276
show ga
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 the PAS. Thus, S174 phosphorylation is
required for formation of autophagosomes, possibly by facilitating the recycling
of Atg9 from the PAS. Our data demonstrate the role of phosphorylation of Atg31
in autophagy.
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