Evidence map›Paper›PMID 32563856›Full record

ReviewCurrent opinion in genetics & development2020

Role of VPS13, a protein with similarity to ATG2, in physiology and disease.

Berrak Ugur, William Hancock-Cerutti, Marianna Leonzino, Pietro De Camilli

Abstract readReview
In one paragraph

Review in Current opinion in genetics & development, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 1 pooled it
–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

47 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
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  18. YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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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

4 authors.

Berrak UgurDepartments of Neuroscience and Cell Biology, Howard Hughes Medical Institute, Program in Cellular Neuroscience, Neurodegeneration and Repair, Kavli Institute for Neuroscience, Yale University School of Medicine, New Haven, CT 06510, USA.
William Hancock-CeruttiDepartments of Neuroscience and Cell Biology, Howard Hughes Medical Institute, Program in Cellular Neuroscience, Neurodegeneration and Repair, Kavli Institute for Neuroscience, Yale University School of Medicine, New Haven, CT 06510, USA.
Marianna LeonzinoDepartments of Neuroscience and Cell Biology, Howard Hughes Medical Institute, Program in Cellular Neuroscience, Neurodegeneration and Repair, Kavli Institute for Neuroscience, Yale University School of Medicine, New Haven, CT 06510, USA.
Pietro De CamilliDepartments of Neuroscience and Cell Biology, Howard Hughes Medical Institute, Program in Cellular Neuroscience, Neurodegeneration and Repair, Kavli Institute for Neuroscience, Yale University School of Medicine, New Haven, CT 06510, USA. Electronic address: pietro.decamilli@yale.edu.

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007205 · NIGMS · YALE UNIVERSITY · PI KAZMIERCZAK, BARBARA I · 1985 to 2019
$42.9M
Yale/NIDA Neuroproteomics Research CenterP30DA018343 · NIDA · YALE UNIVERSITY · PI ANGUS C. NAIRN, Kenneth Robert WILLIAMS · 2004 to 2026
$37.1M
MOLECULAR MECHANISMS IN SYNAPTIC VESICLE RECYCLINGR01NS036251 · NINDS · YALE UNIVERSITY · PI DE CAMILLI, PIETRO · 1997 to 2021
$4.7M
Molecular Mechanisms in Synaptic Vesicle RecyclingR37NS036251 · NINDS · YALE UNIVERSITY · PI DE CAMILLI, PIETRO · 2010 to 2016
$2.7M
Investigating the lipid transport properties of VPS13C at membrane contact sites in relation to Parkinsons Disease pathogenesisF31NS110229 · NINDS · YALE UNIVERSITY · PI HANCOCK-CERUTTI, WILLIAM FRANKLIN · 2018 to 2020
$60k
NIDA NIH HHS P30 DA018343NIGMS NIH HHS T32 GM007205NINDS NIH HHS F31 NS110229NINDS NIH HHS R01 NS036251NINDS NIH HHS R37 NS036251
6 · The paper itself

Abstract

The evolutionarily conserved VPS13 family proteins have been implicated in several cellular processes. Mutations in each of the four human VPS13s cause neurodevelopmental or neurodegenerative disorders. Until recently, the molecular function of VPS13 remained elusive. Genetic, functional and structural studies have now revealed that VPS13 acts at contact sites between intracellular organelles to transport lipids by a novel mechanism: direct transfer between bilayers via a hydrophobic channel that spans its entire rod-like N-terminal half. Predicted similarities to the autophagy protein ATG2 suggested a similar role for ATG2 that has now been confirmed by structural and functional studies. Here, after a brief review of this evidence, we discuss what is known of human VPS13 proteins in physiology and disease.

Indexed as

Autophagy-Related ProteinsBrainHumansNeurodegenerative DiseasesNeurodevelopmental DisordersVesicular Transport ProteinsAutophagy-Related ProteinsVesicular Transport ProteinsVPS13A protein, human

Identifiers

PMID32563856
PMCPMC7746581

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.