Evidence map›Paper›PMID 38491121›Full record

ArticleCommunications biology2024

Identification of membrane curvature sensing motifs essential for VPS37A phagophore recruitment and autophagosome closure.

Yansheng Ye, Xinwen Liang, Guifang Wang, Maria C Bewley, Kouta Hamamoto, Xiaoming Liu, John M Flanagan, Hong-Gang Wang, Yoshinori Takahashi, Fang Tian

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

7 citing papers in PubMed, 7 citations in OpenAlex.

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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

10 authors at 1 institution in 1 country.

Yansheng Ye *Department of Biochemistry and Molecular Biology, The Pennsylvania State University, Hershey, PA, 17033, USA. yanshengye@pennstatehealth.psu.edu.ORCID 0000-0001-9478-6056
Xinwen Liang *Department of Pediatrics, Division of Pediatric Hematology and Oncology, Pennsylvania State University College of Medicine, Hershey, PA, 17033, USA.
Guifang WangDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, Hershey, PA, 17033, USA.
Maria C BewleyDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, Hershey, PA, 17033, USA.ORCID 0000-0001-7097-0123
Kouta HamamotoDepartment of Pediatrics, Division of Pediatric Hematology and Oncology, Pennsylvania State University College of Medicine, Hershey, PA, 17033, USA.
Xiaoming LiuDepartment of Pediatrics, Division of Pediatric Hematology and Oncology, Pennsylvania State University College of Medicine, Hershey, PA, 17033, USA.
John M FlanaganDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, Hershey, PA, 17033, USA.
Hong-Gang WangDepartment of Pediatrics, Division of Pediatric Hematology and Oncology, Pennsylvania State University College of Medicine, Hershey, PA, 17033, USA.ORCID 0000-0003-0551-0571
Yoshinori TakahashiDepartment of Pediatrics, Division of Pediatric Hematology and Oncology, Pennsylvania State University College of Medicine, Hershey, PA, 17033, USA. ytakahashi@pennstatehealth.psu.edu.ORCID 0000-0002-8004-4817
Fang TianDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, Hershey, PA, 17033, USA. ftian@psu.edu.ORCID 0000-0002-5881-6155
Pennsylvania State University · US

Funding

Non-canonical Caspase-8 Activation on Autophagosomal MembranesR01CA222349 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI HONG-GANG WANG · 2018 to 2026
$3.0M
Autophagosome closure by the ESCRT machineryR01GM127954 · NIGMS · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI WANG, HONG-GANG · 2018 to 2025
$2.7M
Structural and Molecular Basis of Human ATG3 Activation and Regulation for LC3 Lipid Conjugation in AutophagyR01GM127730 · NIGMS · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI TIAN, FANG · 2019 to 2022
$1.7M
NCI NIH HHS R01 CA222349NIGMS NIH HHS R01 GM127730NIGMS NIH HHS R01 GM127954
6 · The paper itself

Abstract

VPS37A, an ESCRT-I complex component, is required for recruiting a subset of ESCRT proteins to the phagophore for autophagosome closure. However, the mechanism by which VPS37A is targeted to the phagophore remains obscure. Here, we demonstrate that the VPS37A N-terminal domain exhibits selective interactions with highly curved membranes, mediated by two membrane-interacting motifs within the disordered regions surrounding its Ubiquitin E2 variant-like (UEVL) domain. Site-directed mutations of residues in these motifs disrupt ESCRT-I localization to the phagophore and result in defective phagophore closure and compromised autophagic flux in vivo, highlighting their essential role during autophagy. In conjunction with the UEVL domain, we postulate that these motifs guide a functional assembly of the ESCRT machinery at the highly curved tip of the phagophore for autophagosome closure. These results advance the notion that the distinctive membrane architecture of the cup-shaped phagophore spatially regulates autophagosome biogenesis.

Indexed as

AutophagosomesAutophagyEndosomal Sorting Complexes Required for TransportEndosomesIntracellular MembranesEndosomal Sorting Complexes Required for Transport

Identifiers

PMID38491121
PMCPMC10942982
OpenAlexW4392865138

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.