Evidence map›Paper›PMID 41299140›Full record

ArticleNature structural & molecular biology2026

TMEM170 proteins are lipid scramblases associated with bridge-type lipid transporters BLTP1/Csf1.

Cristian Rocha-Roa, Paige Chandran Blair, Gurpreet Sidhu, Daniel Álvarez, Michael Davey, Elizabeth Conibear, Stefano Vanni

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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
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

7 authors.

Cristian Rocha-RoaDepartment of Biology, University of Fribourg, Fribourg, Switzerland.ORCID http://orcid.org/0000-0002-4602-6121
Paige Chandran BlairCentre for Molecular Medicine and Therapeutics, British Columbia Children's Hospital Research Institute, University of British Columbia, Vancouver, British Columbia, Canada.ORCID http://orcid.org/0009-0009-8422-6253
Gurpreet SidhuCentre for Molecular Medicine and Therapeutics, British Columbia Children's Hospital Research Institute, University of British Columbia, Vancouver, British Columbia, Canada.ORCID http://orcid.org/0009-0005-1830-0620
Daniel ÁlvarezDepartment of Biology, University of Fribourg, Fribourg, Switzerland.ORCID http://orcid.org/0000-0002-8918-9916
Michael DaveyCentre for Molecular Medicine and Therapeutics, British Columbia Children's Hospital Research Institute, University of British Columbia, Vancouver, British Columbia, Canada.ORCID http://orcid.org/0000-0002-1172-5934
Elizabeth ConibearCentre for Molecular Medicine and Therapeutics, British Columbia Children's Hospital Research Institute, University of British Columbia, Vancouver, British Columbia, Canada. conibear@cmmt.ubc.ca.ORCID http://orcid.org/0000-0001-5129-0499
Stefano VanniDepartment of Biology, University of Fribourg, Fribourg, Switzerland. stefano.vanni@unifr.ch.ORCID http://orcid.org/0000-0003-2146-1140

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bulk lipid transport between organelles has been proposed to involve the partnership between bridge-like lipid transfer proteins (BLTPs) and membrane-embedded lipid scramblases. However, for almost all BLTPs, such physical association has not been fully described and, in most cases, the identity of the scramblases is unknown. Here we identify TMEM170-family proteins as endoplasmic reticulum lipid scramblases that physically interact with BLTP1/Csf1 proteins and we provide a revised model detailing the structure of this protein complex in Caenorhabditis elegans. This finding opens avenues to understand the mechanistic basis of lipid transport at membrane contact sites.

Indexed as

Caenorhabditis elegansCaenorhabditis elegans ProteinsPhospholipid Transfer ProteinsAnimalsEndoplasmic ReticulumHumansModels, MolecularCaenorhabditis elegans ProteinsPhospholipid Transfer Proteins

Identifiers

What OpenQuestion holds

Textmetadata
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.