Evidence map›Paper›PMID 40295771›Full record

ArticleNature structural & molecular biology2025

Recruitment of Atg1 to the phagophore by Atg8 orchestrates autophagy machineries.

Jing-Zhen Song, Hui Li, Haiyan Yang, Rui Liu, Wenting Zhang, Tianlong He, Meng-Xi Xie, Chen Chen, Li Cui, Shian Wu and 7 more

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Role of autophagy in antiviral innate immunity.Cellular & molecular biology letters · 2026
    Review
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors.

Jing-Zhen Song *State Key Laboratory of Microbial Metabolism and Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.ORCID http://orcid.org/0000-0002-7074-465X
Hui Li *State Key Laboratory of Microbial Metabolism and Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.ORCID http://orcid.org/0000-0002-2511-910X
Haiyan YangKey Laboratory of Spine and Spinal Cord Injury Repair and Regeneration of Ministry of Education, Orthopedic Department of Tongji Hospital, School of Medicine, Tongji University, Shanghai, China.
Rui LiuState Key Laboratory of Microbial Metabolism and Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Wenting ZhangCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, China.
Tianlong HeCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, China.ORCID http://orcid.org/0009-0007-3083-0151
Meng-Xi XieState Key Laboratory of Microbial Metabolism and Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Chen ChenState Key Laboratory of Microbial Metabolism and Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Li CuiState Key Laboratory of Microbial Metabolism and Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Shian WuSchool of Life Sciences, Nankai University, Tianjin, China.ORCID http://orcid.org/0000-0003-4990-6594
Yueguang RongSchool of Basic Medicine, Huazhong University of Science and Technology, Wuhan, China.
Li-Feng PanShanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0002-9229-6288
Jing ZhuState Key Laboratory of Microbial Metabolism and Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Qingqiu GongState Key Laboratory of Microbial Metabolism and Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China. gongqingqiu@sjtu.edu.cn.ORCID http://orcid.org/0000-0002-9803-8554
Juan WangCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, China. juanwang@bjut.edu.cn.ORCID http://orcid.org/0009-0002-9208-7985
Zhao QinKey Laboratory of Spine and Spinal Cord Injury Repair and Regeneration of Ministry of Education, Orthopedic Department of Tongji Hospital, School of Medicine, Tongji University, Shanghai, China. zqin.med@tongji.edu.cn.ORCID http://orcid.org/0000-0003-1709-0818
Zhiping XieState Key Laboratory of Microbial Metabolism and Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China. zxie@sjtu.edu.cn.ORCID http://orcid.org/0000-0001-5816-6159

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy-related (Atg) proteins catalyze autophagosome formation at the phagophore assembly site (PAS). The assembly of Atg proteins at the PAS follows a semihierarchical order, in which Atg8 is thought to be quite downstream but still able to control the size of autophagosomes. Yet, how Atg8 coordinates multiple branches of autophagy machinery to regulate autophagosomal size is not clear. Here, we show that, in yeast, Atg8 positively regulates the autophagy-specific phosphatidylinositol 3-OH kinase complex and the retrograde trafficking of Atg9 vesicles through interaction with Atg1. Mechanistically, Atg8 does not enhance the kinase activity of Atg1; instead, it recruits Atg1 to the surface of the phagophore likely to orient Atg1's activity toward select substrates, leading to efficient phagophore expansion. Artificial tethering of Atg1 kinase domains to Atg8s enhanced autophagy in yeast, human and plant cells and improved muscle performance in worms. We propose that Atg8-mediated relocation of Atg1 from the PAS scaffold to the phagophore is a critical step in positive autophagy regulation.

Indexed as

AutophagosomesAutophagyAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAnimalsHumansMembrane ProteinsProtein KinasesATG1 protein, S cerevisiaeATG8 protein, S cerevisiaeATG9 protein, S cerevisiaeAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsMembrane ProteinsProtein KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID40295771

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.