Evidence map›Paper›PMID 39913206›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Mec1-mediated Atg9 phosphorylation regulates the PAS recruitment of Atg9 vesicles upon energy stress.

Siyu Fan, Shuling Dong, Weijing Yao, Yi Zhang, Mingzhu Fan, Shan Feng, Choufei Wu, Liqin Zhang, Cong Yi

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. bioRxiv : the preprint server for biology · 2026
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Siyu FanDepartment of Biochemistry and Department of Hepatobiliary and Pancreatic Surgery of the First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.ORCID 0009-0006-8228-4060
Shuling DongBiology Department, Key Laboratory of Vector Biology and Pathogen Control of Zhejiang Province, School of Life Sciences, Huzhou University, Huzhou 313000, China.
Weijing YaoDepartment of Biochemistry and Department of Hepatobiliary and Pancreatic Surgery of the First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
Yi ZhangDepartment of Biochemistry and Department of Hepatobiliary and Pancreatic Surgery of the First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
Mingzhu FanMass Spectrometry & Metabolomics Core Facility, Key Laboratory of Structural Biology of Zhejiang Province, Westlake University, Hangzhou 310030, China.
Shan FengMass Spectrometry & Metabolomics Core Facility, Key Laboratory of Structural Biology of Zhejiang Province, Westlake University, Hangzhou 310030, China.
Choufei WuBiology Department, Key Laboratory of Vector Biology and Pathogen Control of Zhejiang Province, School of Life Sciences, Huzhou University, Huzhou 313000, China.
Liqin ZhangBiology Department, Key Laboratory of Vector Biology and Pathogen Control of Zhejiang Province, School of Life Sciences, Huzhou University, Huzhou 313000, China.
Cong YiDepartment of Biochemistry and Department of Hepatobiliary and Pancreatic Surgery of the First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.ORCID 0000-0001-6853-6563

Funding

MOST | National Key Research and Development Program of China (NKPs) 2021YFC2600104MOST | National Natural Science Foundation of China (NSFC) 32100600MOST | National Natural Science Foundation of China (NSFC) 32122028;92254307;32070739
6 · The paper itself

Abstract

Mec1 plays an essential role in both the DNA damage response and glucose starvation-induced autophagy. We recently reported that Mec1 regulates glucose starvation-induced autophagy through its direct binding to Atg13. However, the role of Mec1's kinase activity in autophagy remains unclear. In this study, we demonstrate that the kinase activity of Mec1 is required for glucose starvation-induced autophagy by regulating the phagophore assembly site (PAS) recruitment of Atg9 vesicles. Mechanistic and functional analyses identified Atg9 as a direct phosphorylation substrate of Mec1, with phosphorylation occurring at the S35, T203, and T243 sites. Mutations at these sites reduce the association of Atg9 with Atg17, Atg23, and Atg27, thereby impairing the PAS recruitment of Atg9 vesicles. Notably, we found that the Mec1-Atg13 binding is a prerequisite for the phosphorylation of Atg9 by Mec1. Furthermore, Mec1-mediated phosphorylation of Atg9 is also crucial for the PAS recruitment of Atg9 vesicles in response to DNA damage. We thus propose that Mec1's kinase activity regulates the PAS recruitment of Atg9 vesicles by phosphorylating Atg9 in response to energy stress and DNA damage.

Indexed as

AutophagosomesAutophagy-Related ProteinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStress, PhysiologicalAdaptor Proteins, Signal TransducingAutophagyGlucosePhosphorylationAdaptor Proteins, Signal TransducingATG13 protein, S cerevisiaeATG9 protein, S cerevisiaeAutophagy-Related ProteinsGlucoseIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeMembrane ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsAtg9DNA damage–induced autophagyglucose starvation–induced autophagyMec1Saccharomyces cerevisiae

Identifiers

PMID39913206
PMCPMC11831128

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.