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EMBO Rep. 2015 Jul;16(7):824-35. doi: 10.15252/embr.201540229. Epub 2015 Jun 12.

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

Author information

1
Department of Life Sciences, Imperial College London, London, UK.
2
Department of Life Sciences, Imperial College London, London, UK School of Biological and Chemical Sciences, Joseph Priestley Building Queen Mary University of London, London, UK.
3
Institute for Genetics, Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Center for Molecular Medicine (CMMC), University of Cologne, Cologne, Germany.
4
Department of Surgery and Cancer, Imperial College London, Hammersmith Hospital Campus, London, UK.
5
Department of Life Sciences, Imperial College London, London, UK s.j.matthews@imperial.ac.uk.

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.

PMID:
26071602
PMCID:
PMC4515122
DOI:
10.15252/embr.201540229
[Indexed for MEDLINE]
Free PMC Article

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