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Structural comparison of yeast and human intra-mitochondrial lipid transport systems

DOI: 10.1042/BST20150264 DOI Help

Authors: Xeni Miliara (Imperial College London) , Stephen Matthews (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemical Society Transactions , VOL 44 , PAGES 479 - 485

State: Published (Approved)
Published: April 2016
Diamond Proposal Number(s): 9424 , 12579

Open Access Open Access

Abstract: Mitochondria depend on a tightly regulated supply of phospholipids. The protein of relevant evolutionary and lymphoid interest (PRELI)/Ups1 family together with its mitochondrial chaperones [TP53-regulated inhibitor of apoptosis 1 (TRIAP1)/Mdm35] represents a unique heterodimeric lipid-transfer system that is evolutionary conserved from yeast to man. Recent X-ray crystal structures of the human and yeast systems are compared and discuss here and shed new insight into the mechanism of the PRELI/Ups1 system.

Subject Areas: Medicine


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography