Very-long-chain acyl-CoA dehydrogenase subunit assembles to the dimer form on mitochondrial inner membrane

FEBS Lett. 1998 Apr 17;426(2):187-90. doi: 10.1016/s0014-5793(98)00343-3.


This paper describes the process of dimer assembly of mitochondrial very-long-chain acyl-CoA dehydrogenase (VLCAD) subunit. Mature VLCAD is a homodimer of a 70-kDa protein associated with the mitochondrial membrane. Newly synthesized VLCAD was present as a monomer and the major fraction was associated with the mitochondrial inner membrane. The association of VLCAD subunit with the mitochondrial membrane was observed early during dimer formation. In contrast, a VLCAD monomeric mutant S583W, a novel mutation identified from a patient with VLCAD deficiency, did not associate with the mitochondrial membrane after import and the major fraction remained in the mitochondrial matrix. These results suggest that association of VLCAD protein with mitochondrial inner membrane is necessary for dimer assembly and formation of mature VLCAD.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl-CoA Dehydrogenase, Long-Chain
  • Acyl-CoA Dehydrogenases / deficiency
  • Acyl-CoA Dehydrogenases / metabolism*
  • Cell Compartmentation
  • Dimerization
  • Female
  • Heterozygote
  • Humans
  • Infant
  • Intracellular Membranes / enzymology
  • Lipid Metabolism, Inborn Errors / enzymology
  • Lipid Metabolism, Inborn Errors / genetics
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Mitochondria / enzymology*
  • Mitochondria / ultrastructure
  • Structure-Activity Relationship


  • Membrane Proteins
  • Acyl-CoA Dehydrogenases
  • Acyl-CoA Dehydrogenase, Long-Chain