Evidence map›Paper›PMID 35267021›Full record

ReviewJournal of cell science2022

A possible role for VPS13-family proteins in bulk lipid transfer, membrane expansion and organelle biogenesis.

Thomas J Melia, Karin M Reinisch

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

35 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. The molecular mechanism of lipid uptake by membrane-anchored bridge-like lipid transfer proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. The Diverse Neuromuscular Spectrum of VPS13A Disease.Annals of clinical and translational neurology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Stairway to the Golgi: Two paths VPS13B can go by.The Journal of cell biology · 2024
    Article
  12. Article
  13. Review
  14. Lipid scrambling is a general feature of protein insertases.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Sorting of complex sphingolipids within the cellular endomembrane systems.Frontiers in cell and developmental biology · 2024
    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

2 authors at 1 institution in 1 country.

Thomas J MeliaDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520, USA.ORCID 0000-0002-5798-4624
Karin M ReinischDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520, USA.ORCID 0000-0001-9140-6150
Yale University · US

Funding

Molecular Basis for Membrane Lipid HomeostasisR35GM131715 · NIGMS · YALE UNIVERSITY · PI KARIN M REINISCH · 2019 to 2026
$6.5M
Lipid flux during autophagosome membrane biogenesisR01GM135290 · NIGMS · YALE UNIVERSITY · PI MELIA, THOMAS JAMES · 2020 to 2023
$1.3M
Aligning Science Across Parkinson's ASAP-000580NIGMS NIH HHS R01 GM135290NIGMS NIH HHS R35 GM131715
6 · The paper itself

Abstract

At organelle-organelle contact sites, proteins have long been known to facilitate the rapid movement of lipids. Classically, this lipid transport involves the extraction of single lipids into a hydrophobic pocket on a lipid transport protein. Recently, a new class of lipid transporter has been described with physical characteristics that suggest these proteins are likely to function differently. They possess long hydrophobic tracts that can bind many lipids at once and physically span the entire gulf between membranes at contact sites, suggesting that they may act as bridges to facilitate bulk lipid flow. Here, we review what has been learned regarding the structure and function of this class of lipid transporters, whose best characterized members are VPS13 and ATG2 proteins, and their apparent coordination with other lipid-mobilizing proteins on organelle membranes. We also discuss the prevailing hypothesis in the field, that this type of lipid transport may facilitate membrane expansion through the bulk delivery of lipids, as well as other emerging hypotheses and questions surrounding these novel lipid transport proteins.

Indexed as

Mitochondrial MembranesOrganelle BiogenesisCarrier ProteinsLipidsMembranesProteinsCarrier ProteinsLipidsProteinsMembrane contact sitesMembrane homeostasisProtein-mediated lipid transport

Identifiers

PMID35267021
PMCPMC8976877
OpenAlexW4221056627

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.