Evidence map›Paper›PMID 35491307›Full record

ReviewTrends in cell biology2022

A novel superfamily of bridge-like lipid transfer proteins.

Sarah D Neuman, Tim P Levine, Arash Bashirullah

Abstract readReview
In one paragraph

Review in Trends in cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
–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

69 citing papers in PubMed.

  1. Article
  2. bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026
    Review
  6. Article
  7. Mechanistic dissection of BLTP2 targeting to ER-PM contact sites.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. YdbL directly modulates YdbH-YnbE bridge formation to maintainbioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. 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
  13. Impacts of Globo H Ceramide on Tumor Microenvironment.Advances in experimental medicine and biology · 2026
    Review
  14. Review
  15. Article
  16. Article
  17. Bltp1 Is Required for Survival and Normal Development and Function of the Neuromuscular Junction in Mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  18. Article
  19. Article
  20. Review

9 more citing papers are in PubMed but not listed here.

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

3 authors.

Sarah D NeumanDivision of Pharmaceutical Sciences, University of Wisconsin-Madison, Madison, WI 53705-2222, USA.
Tim P LevineUCL Institute of Ophthalmology, University College London, 11-43 Bath Street, London, EC1V 9EL, UK. Electronic address: tim.levine@ucl.ac.uk.
Arash BashirullahDivision of Pharmaceutical Sciences, University of Wisconsin-Madison, Madison, WI 53705-2222, USA. Electronic address: bashirullah@wisc.edu.

Funding

Genetic analysis of regulated exocytosis during Drosophila developmentR01GM123204 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BASHIRULLAH, ARASH · 2017 to 2020
$1.4M
Biotechnology and Biological Sciences Research Council BB/P003818/1NIGMS NIH HHS R01 GM123204
6 · The paper itself

Abstract

Lipid transfer proteins mediate nonvesicular transport of lipids at membrane contact sites to regulate the lipid composition of organelle membranes. Recently, a new type of bridge-like lipid transfer protein has emerged; these proteins contain a long hydrophobic groove and can mediate bulk transport of lipids between organelles. Here, we review recent insights into the structure of these proteins and identify a repeating modular unit that we propose to name the repeating β-groove (RBG) domain. This new structural understanding conceptually unifies all the RBG domain-containing lipid transfer proteins as members of an RBG protein superfamily. We also examine the biological functions of these lipid transporters in normal physiology and disease and speculate on the evolutionary origins of RBG proteins in bacteria.

Indexed as

Carrier ProteinsMitochondrial MembranesHumansLipid MetabolismLipidsOrganellesCarrier ProteinsLipidslipid transfer proteinAlphaFoldautophagylipidslipid transfer proteinsmembrane contact sitesVps13

Identifiers

PMID35491307
PMCPMC9588498

What OpenQuestion holds

Textmetadata
LicenceTDM
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.