Evidence map›Paper›PMID 42156739›Full record

ArticleNature communications2026

Lipid metabolism and contact site homologs are present at the chloroplast envelope-thylakoid interface.

Evan W LaBrant, Cailin N Smith, Alondra D Torres-Gerena, Joslin Ishimwe, Fan Huang, Allan Tullis, Lauren Litterer, Bhoomi F Modi, Michael J Naldrett, Bara Altartouri and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

11 authors.

Evan W LaBrant *Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.
Cailin N Smith *Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.ORCID http://orcid.org/0000-0002-0188-806X
Alondra D Torres-GerenaDepartment of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.ORCID http://orcid.org/0000-0003-4674-1800
Joslin IshimweDepartment of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.
Fan HuangDepartment of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.
Allan TullisDepartment of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.
Lauren LittererDepartment of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.
Bhoomi F ModiDepartment of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.
Michael J NaldrettProteomics and Metabolomics Facility, Center for Biotechnology, University of Nebraska-Lincoln, Lincoln, NE, USA.ORCID http://orcid.org/0000-0002-6899-5652
Bara AltartouriDepartment of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.ORCID http://orcid.org/0000-0002-9148-640X
Rebecca L RostonDepartment of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE, USA. rroston@unl.edu.ORCID http://orcid.org/0000-0002-3063-5002

Funding

U.S. Department of Energy (DOE) DE-SC0021101
6 · The paper itself

Abstract

Biogenesis and maintenance of the photosynthetic thylakoid membrane requires transport of lipids from their site of synthesis in the chloroplast envelopes to their destination in the thylakoid. While vesicle trafficking is likely involved, we hypothesized a complementary mechanism involving direct membrane interactions. Using domain homology and proteomic profiling of chloroplast membrane fractions, we identified candidate lipid transport proteins present in a distinct, intermediate-density membrane population. This fraction contained an overrepresentation of lipid metabolic enzymes and proteins homologous to known membrane organization factors. Several candidates, including TVP38 FAMILY PROTEIN (TVPFP), PLASMA MEMBRANE FUSION PROTEIN (PMFP), and LETM1-LIKE, localized to discrete subdomains within chloroplasts. Loss-of-function tvpfp or pmfp mutants exhibited altered chloroplast ultrastructure, including changes in thylakoid-envelope proximity, supporting their roles in maintaining membrane architecture. These findings, which identify a chloroplast membrane subdomain enriched in proteins with specialized functions, offer a foundation for elucidating the molecular architecture of these regions.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsLipid MetabolismThylakoidsIntracellular MembranesMembrane ProteinsMutationProteomicsArabidopsis ProteinsMembrane Proteins

Identifiers

PMID42156739
PMCPMC13381928

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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.