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

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. © 2015 The Authors. Published under the terms of the CC BY 4.0 license.

Citation

Xeni Miliara, James A Garnett, Takashi Tatsuta, Ferdos Abid Ali, Heather Baldie, Inmaculada Pérez-Dorado, Peter Simpson, Ernesto Yague, Thomas Langer, Stephen Matthews. Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes. EMBO reports. 2015 Jul;16(7):824-35

Mesh Tags

Substances

PMID: 26071602

search → result