Structural insight into the TRIAP1/PRELI‐like domain family of mitochondrial phospholipid transfer complexes. (13th June 2015)

• Record Type: Journal Article
• Authors: Miliara, Xeni; Garnett, James A; Tatsuta, Takashi; Abid Ali, Ferdos; Baldie, Heather; Pérez‐Dorado, Inmaculada; Simpson, Peter; Yague, Ernesto; Langer, Thomas; Matthews, Stephen
• Is Part Of: EMBO reports. Volume 16:Number 7(2015:Jul.)
• Page Start: 824
• Page End: 835
• Publication Date: 2015-06-13
• Subjects: Molecular biology -- Periodicals; Molecular Biology -- Periodicals; Molecular biology; Periodicals; 572.8
• DOI: 10.15252/embr.201540229
• Languages: English
• ISSNs: 1469-221X

Abstract

<abstract abstract-type="main" id="embr201540229-abs-0001"> <title>Abstract</title> <p>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.</p> </abstract>