Evidence map›Paper›PMID 26410300›Full record

ArticleThe Plant cell2015

Arabidopsis TRIGALACTOSYLDIACYLGLYCEROL5 Interacts with TGD1, TGD2, and TGD4 to Facilitate Lipid Transfer from the Endoplasmic Reticulum to Plastids.

Jilian Fan, Zhiyang Zhai, Chengshi Yan, Changcheng Xu

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

55 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
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  3. Mce transport systems inJournal of bacteriology · 2026
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  6. Review
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  9. Genome-Wide Identification and Expression Profiling ofInternational journal of molecular sciences · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Plastid Transient and Stable Interactions with Other Cell Compartments.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. Article
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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.

Jilian FanBiological, Environmental, and Climate Sciences Department, Brookhaven National Laboratory, Upton, New York 11973.ORCID http://orcid.org/0000-0002-6821-6583
Zhiyang ZhaiBiological, Environmental, and Climate Sciences Department, Brookhaven National Laboratory, Upton, New York 11973.ORCID http://orcid.org/0000-0003-3181-1773
Chengshi YanBiological, Environmental, and Climate Sciences Department, Brookhaven National Laboratory, Upton, New York 11973.
Changcheng XuBiological, Environmental, and Climate Sciences Department, Brookhaven National Laboratory, Upton, New York 11973 cxu@bnl.gov.ORCID http://orcid.org/0000-0002-0179-9462
Brookhaven National Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biogenesis of photosynthetic membranes in the plastids of higher plants requires an extensive supply of lipid precursors from the endoplasmic reticulum (ER). Four TRIGALACTOSYLDIACYLGLYCEROL (TGD) proteins (TGD1,2,3,4) have thus far been implicated in this lipid transfer process. While TGD1, TGD2, and TGD3 constitute an ATP binding cassette transporter complex residing in the plastid inner envelope, TGD4 is a transmembrane lipid transfer protein present in the outer envelope. These observations raise questions regarding how lipids transit across the aqueous intermembrane space. Here, we describe the isolation and characterization of a novel Arabidopsis thaliana gene, TGD5. Disruption of TGD5 results in similar phenotypic effects as previously described in tgd1,2,3,4 mutants, including deficiency of ER-derived thylakoid lipids, accumulation of oligogalactolipids, and triacylglycerol. Genetic analysis indicates that TGD4 is epistatic to TGD5 in ER-to-plastid lipid trafficking, whereas double mutants of a null tgd5 allele with tgd1-1 or tgd2-1 show a synergistic embryo-lethal phenotype. TGD5 encodes a small glycine-rich protein that is localized in the envelope membranes of chloroplasts. Coimmunoprecipitation assays show that TGD5 physically interacts with TGD1, TGD2, TGD3, and TGD4. Collectively, these results suggest that TGD5 facilitates lipid transfer from the outer to the inner plastid envelope by bridging TGD4 with the TGD1,2,3 transporter complex.

Indexed as

Adenosine TriphosphatasesArabidopsisArabidopsis ProteinsBiological TransportCarrier ProteinsEndoplasmic ReticulumEpistasis, GeneticIntracellular MembranesLipid MetabolismMembrane Transport ProteinsMesophyll CellsMutationPhenotypePlastidsProtein BindingThylakoidsAdenosine TriphosphatasesArabidopsis ProteinsCarrier Proteinslipid transfer proteinMembrane Transport ProteinsTGD1 protein, ArabidopsisTGD2 protein, ArabidopsisTGD3 protein, ArabidopsisTGD4 protein, ArabidopsisTGD5 protein, Arabidopsis

Identifiers

PMID26410300
PMCPMC4682317
OpenAlexW2189085830

What OpenQuestion holds

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Registered trials

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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.