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

Miliara, X.; Garnett, J. A.; Tatsuta, T.; Abid Ali, F.; Baldie, H.; Perez-Dorado, I.; Simpson, P.; Yague, E.; Langer, T.; Matthews, S.

doi:10.15252/embr.201540229

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

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Tatsuta, T.
Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society;

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Langer, T.
Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society;

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https://www.ncbi.nlm.nih.gov/pubmed/26071602
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Citation

Miliara, X., Garnett, J. A., Tatsuta, T., Abid Ali, F., Baldie, H., Perez-Dorado, I., et al. (2015). Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes. EMBO Rep, 16(7), 824-35. doi:10.15252/embr.201540229.

Cite as: https://hdl.handle.net/21.11116/0000-000B-7ADA-7

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.