Evidence map›Paper›PMID 26071602›Full record

ArticleEMBO reports2015

Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes.

Xeni Miliara, James A Garnett, Takashi Tatsuta, Ferdos Abid Ali, Heather Baldie, Inmaculada Pérez-Dorado, Peter Simpson, Ernesto Yague, Thomas Langer, Stephen Matthews

Abstract read
In one paragraph

Article in EMBO reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Mitochondrial heterogeneity in diseases.Signal transduction and targeted therapy · 2023
    Review
  8. Non-Vesicular Lipid Transport Machinery inInternational journal of molecular sciences · 2023
    Review
  9. Review
  10. Review
  11. Article
  12. Altered Mitochondrial Protein Homeostasis and Proteinopathies.Frontiers in molecular neuroscience · 2022
    Review
  13. Article
  14. Courier service for phosphatidylinositol: PITPs deliver on demand.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020
    Review
  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

10 authors.

Xeni MiliaraDepartment of Life Sciences, Imperial College London, London, UK.
James A GarnettDepartment of Life Sciences, Imperial College London, London, UK School of Biological and Chemical Sciences, Joseph Priestley Building Queen Mary University of London, London, UK.
Takashi TatsutaInstitute for Genetics, Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Center for Molecular Medicine (CMMC), University of Cologne, Cologne, Germany.
Ferdos Abid AliDepartment of Life Sciences, Imperial College London, London, UK.
Heather BaldieDepartment of Life Sciences, Imperial College London, London, UK.
Inmaculada Pérez-DoradoDepartment of Life Sciences, Imperial College London, London, UK.
Peter SimpsonDepartment of Life Sciences, Imperial College London, London, UK.
Ernesto YagueDepartment of Surgery and Cancer, Imperial College London, Hammersmith Hospital Campus, London, UK.
Thomas LangerInstitute for Genetics, Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Center for Molecular Medicine (CMMC), University of Cologne, Cologne, Germany.
Stephen MatthewsDepartment of Life Sciences, Imperial College London, London, UK s.j.matthews@imperial.ac.uk.

Funding

Medical Research Council MR/J006874/1Medical Research Council MR/M019403/1Wellcome Trust
6 · The paper itself

Abstract

The composition of the mitochondrial membrane is important for its architecture and proper function. Mitochondria depend on a tightly regulated supply of phospholipid via intra-mitochondrial synthesis and by direct import from the endoplasmic reticulum. The Ups1/PRELI-like family together with its mitochondrial chaperones (TRIAP1/Mdm35) represent a unique heterodimeric lipid transfer system that is evolutionary conserved from yeast to man. Work presented here provides new atomic resolution insight into the function of a human member of this system. Crystal structures of free TRIAP1 and the TRIAP1-SLMO1 complex reveal how the PRELI domain is chaperoned during import into the intermembrane mitochondrial space. The structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest that they share similar lipid transfer mechanisms, in which access to a buried phospholipid-binding cavity is regulated by conformationally adaptable loops.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceBinding SitesBiological TransportCrystallography, X-RayEndoplasmic ReticulumHumansHydrophobic and Hydrophilic InteractionsIntracellular Signaling Peptides and ProteinsMembrane ProteinsMitochondriaMitochondrial MembranesMitochondrial ProteinsMolecular ChaperonesMolecular Sequence DataPhospholipidsAdaptor Proteins, Signal TransducingAPBB1IP protein, humanIntracellular Signaling Peptides and ProteinsMembrane ProteinsMitochondrial ProteinsMolecular ChaperonesPhospholipidsTRIAP1 protein, human

Identifiers

PMID26071602
PMCPMC4515122

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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.