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

Biochem Soc Trans. 2016 Apr 15;44(2):479-85. doi: 10.1042/BST20150264.

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.

Keywords: PRELI; TRIAP1; Ups1; membranes; mitochondria; phospholipid transport.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry
  • Adaptor Proteins, Signal Transducing / metabolism
  • Amino Acid Sequence
  • Biological Transport
  • Crystallography, X-Ray
  • Humans
  • Lipids*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Mitochondria / metabolism*
  • Models, Molecular
  • Phylogeny
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Yeasts / metabolism*

Substances

  • APBB1IP protein, human
  • Adaptor Proteins, Signal Transducing
  • Lipids
  • Membrane Proteins