Volume 6 Issue 4
Apr.  2015
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Wenzhi Feng, Tong Wu, Xiaoyu Dan, Yuling Chen, Lin Li, She Chen, Di Miao, Haiteng Deng, Xinqi Gong, Li Yu. Phosphorylation of Atg31 is required for autophagy[J]. Protein&Cell, 2015, 6(4): 288-296. doi: 10.1007/s13238-015-0138-4
Citation: Wenzhi Feng, Tong Wu, Xiaoyu Dan, Yuling Chen, Lin Li, She Chen, Di Miao, Haiteng Deng, Xinqi Gong, Li Yu. Phosphorylation of Atg31 is required for autophagy[J]. Protein&Cell, 2015, 6(4): 288-296. doi: 10.1007/s13238-015-0138-4

Phosphorylation of Atg31 is required for autophagy

doi: 10.1007/s13238-015-0138-4
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This research was supported by the National Natural Science Foundation of China (Grant Nos. 31030043, 30971484 and 31321003), the National Basic Research Program (973 Program) (Nos. 2010CB833704 and 2011CB910100), and Tsinghua University Grants 2010THZ0 and 2009THZ03071 to Li Yu.

  • Received Date: 2014-12-17
  • Rev Recd Date: 2015-01-23
  • 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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