Evidence map›Paper›PMID 27490928›Full record

ArticleCell death & disease2016

TMEM166/EVA1A interacts with ATG16L1 and induces autophagosome formation and cell death.

Jia Hu, Ge Li, Liujing Qu, Ning Li, Wei Liu, Dan Xia, Beiqi Hongdu, Xin Lin, Chentong Xu, Yaxin Lou and 3 more

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
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

37 citing papers in PubMed, 60 citations in OpenAlex.

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  15. The Emerging Role of EVA1A in Different Types of Cancers.International journal of molecular sciences · 2022
    Review
  16. Article
  17. Article
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  19. The lysosome as an imperative regulator of autophagy and cell death.Cellular and molecular life sciences : CMLS · 2021
    Review
  20. Review
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

13 authors at 2 institutions in 1 country.

Jia HuDepartment of Immunology, Peking University School of Basic Medical Science; Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Sciences Center, 38 Xueyuan Road, Beijing 100191, China.
Ge LiDepartment of Immunology, Peking University School of Basic Medical Science; Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Sciences Center, 38 Xueyuan Road, Beijing 100191, China.
Liujing QuDepartment of Immunology, Peking University School of Basic Medical Science; Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Sciences Center, 38 Xueyuan Road, Beijing 100191, China.
Ning LiDepartment of Biochemistry and Molecular Biology, Program in Molecular and Cell Biology, Zhejiang University School of Medicine, 866 Yu-Hang-Tang Road, Hangzhou 310058, China.
Wei LiuDepartment of Biochemistry and Molecular Biology, Program in Molecular and Cell Biology, Zhejiang University School of Medicine, 866 Yu-Hang-Tang Road, Hangzhou 310058, China.
Dan XiaDepartment of Immunology, Peking University School of Basic Medical Science; Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Sciences Center, 38 Xueyuan Road, Beijing 100191, China.
Beiqi HongduDepartment of Immunology, Peking University School of Basic Medical Science; Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Sciences Center, 38 Xueyuan Road, Beijing 100191, China.
Xin LinDepartment of Immunology, Peking University School of Basic Medical Science; Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Sciences Center, 38 Xueyuan Road, Beijing 100191, China.
Chentong XuDepartment of Immunology, Peking University School of Basic Medical Science; Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Sciences Center, 38 Xueyuan Road, Beijing 100191, China.
Yaxin LouMedical and Healthy Analytical Center, Peking University, 38 Xueyuan Road, Beijing 100191, China.
Qihua HeMedical and Healthy Analytical Center, Peking University, 38 Xueyuan Road, Beijing 100191, China.
Dalong MaDepartment of Immunology, Peking University School of Basic Medical Science; Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Sciences Center, 38 Xueyuan Road, Beijing 100191, China.
Yingyu ChenDepartment of Immunology, Peking University School of Basic Medical Science; Key Laboratory of Medical Immunology, Ministry of Health, Peking University Health Sciences Center, 38 Xueyuan Road, Beijing 100191, China.
Peking University · CNZhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The formation of the autophagosome is controlled by an orderly action of ATG proteins. However, how these proteins are recruited to autophagic membranes remain poorly clarified. In this study, we have provided a line of evidence confirming that EVA1A (eva-1 homolog A)/TMEM166 (transmembrane protein 166) is associated with autophagosomal membrane development. This notion is based on dotted EVA1A structures that colocalize with ZFYVE1, ATG9, LC3B, ATG16L1, ATG5, STX17, RAB7 and LAMP1, which represent different stages of the autophagic process. It is required for autophagosome formation as this phenotype was significantly decreased in EVA1A-silenced cells and Eva1a KO MEFs. EVA1A-induced autophagy is independent of the BECN1-PIK3C3 (phosphatidylinositol 3-kinase, catalytic subunit type 3) complex but requires ATG7 activity and the ATG12-ATG5/ATG16L1 complex. Here, we present a molecular mechanism by which EVA1A interacts with the WD repeats of ATG16L1 through its C-terminal and promotes ATG12-ATG5/ATG16L1 complex recruitment to the autophagic membrane and enhances the formation of the autophagosome. We also found that both autophagic and apoptotic mechanisms contributed to EVA1A-induced cell death while inhibition of autophagy and apoptosis attenuated EVA1A-induced cell death. Overall, these findings provide a comprehensive view to our understanding of the pathways involved in the role of EVA1A in autophagy and programmed cell death.

Indexed as

ApoptosisAnimalsAutophagosomesAutophagyAutophagy-Related Protein 5Autophagy-Related ProteinsBeclin-1Cell Line, TumorGene Knockdown TechniquesHumansIntracellular MembranesMembrane ProteinsMiceMicrotubule-Associated ProteinsMutant ProteinsPhosphatidylinositol 3-KinasesATG16L1 protein, humanAutophagy-Related Protein 5Autophagy-Related ProteinsBeclin-1Becn1 protein, mouseEVA1A protein, humanMap1lc3b protein, mouseMembrane ProteinsMicrotubule-Associated ProteinsMutant ProteinsPhosphatidylinositol 3-Kinases

Identifiers

PMID27490928
PMCPMC5108317
OpenAlexW2476750798

What OpenQuestion holds

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LicenceCC BY
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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.