Evidence map›Paper›PMID 35357422›Full record

ArticleThe Journal of cell biology2022

Structural and biochemical insights into lipid transport by VPS13 proteins.

Jyoti Adlakha, Zhouping Hong, PeiQi Li, Karin M Reinisch

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
6.1field-weighted citation impact, top 2% 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

42 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
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  5. Mechanistic dissection of BLTP2 targeting to ER-PM contact sites.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Neurodegenerative and Neurodevelopmental Roles for Bulk Lipid Transporters VPS13A and BLTP2.Movement disorders : official journal of the Movement Disorder Society · 2025
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Lipid scrambling is a general feature of protein insertases.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article
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 at 1 institution in 1 country.

Jyoti Adlakha *Department of Cell Biology, Yale School of Medicine, New Haven, CT.ORCID 0000-0002-3369-1392
Zhouping Hong *Department of Cell Biology, Yale School of Medicine, New Haven, CT.ORCID 0000-0002-8513-3288
PeiQi LiDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Karin M ReinischDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.ORCID 0000-0001-9140-6150
Yale University · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
Molecular Basis for Membrane Lipid HomeostasisR35GM131715 · NIGMS · YALE UNIVERSITY · PI KARIN M REINISCH · 2019 to 2026
$6.5M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
Aligning Science Across Parkinson's ASAP-000580China Scholarship CouncilNIGMS NIH HHS P30 GM124165NIGMS NIH HHS R35 GM131715NIH HHS P30 GM124165NIH HHS S10 OD021527
6 · The paper itself

Abstract

VPS13 proteins are proposed to function at contact sites between organelles as bridges for lipids to move directionally and in bulk between organellar membranes. VPS13s are anchored between membranes via interactions with receptors, including both peripheral and integral membrane proteins. Here we present the crystal structure of VPS13s adaptor binding domain (VAB) complexed with a Pro-X-Pro peptide recognition motif present in one such receptor, the integral membrane protein Mcp1p, and show biochemically that other Pro-X-Pro motifs bind the VAB in the same site. We further demonstrate that Mcp1p and another integral membrane protein that interacts directly with human VPS13A, XK, are scramblases. This finding supports an emerging paradigm of a partnership between bulk lipid transport proteins and scramblases. Scramblases can re-equilibrate lipids between membrane leaflets as lipids are removed from or inserted into the cytosolic leaflet of donor and acceptor organelles, respectively, in the course of protein-mediated transport.

Indexed as

LipidsMitochondrial MembranesVesicular Transport ProteinsAmino Acid MotifsBiological TransportHumansLipidsVesicular Transport ProteinsVPS13A protein, human

Identifiers

PMID35357422
PMCPMC8978259
OpenAlexW4221090868

What Socratic 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 Socratic graph.