Complex I and the cAMP cascade in human physiopathology

Biosci Rep. 2002 Feb;22(1):3-16. doi: 10.1023/a:1016004921277.

Abstract

A cAMP-dependent protein kinase (PKA) is localized in mammalian mitochondria with the catalytic site at the matrix side of the membrane where it phosphorylates a number of proteins. One of these is the 18 kDa(IP) subunit of the mammalian complex I of the respiratory chain, encoded by the nuclear NDUFS4 gene. Mitochondria have a Ca(2+)-inhibited phosphatase, which dephosphorylates the 18 kDa phosphoprotein of complex I. In fibroblast and myoblast cultures cAMP-dependent phosphorylation of the 18 kDa protein is associated with stimulation of complex I and overall respiratory activity with NAD-linked substrates. Mutations in the human NDUFS4 gene have been found, which in the homozygous state are associated with deficiency of complex I and fatal neurological syndrome.

Publication types

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

MeSH terms

  • Base Sequence
  • Cyclic AMP / metabolism*
  • Electron Transport Complex I
  • Humans
  • Mitochondrial Diseases / metabolism*
  • Mitochondrial Diseases / physiopathology*
  • Molecular Sequence Data
  • NADH, NADPH Oxidoreductases / genetics*
  • NADH, NADPH Oxidoreductases / metabolism*
  • Sequence Homology, Amino Acid

Substances

  • Cyclic AMP
  • NADH, NADPH Oxidoreductases
  • Electron Transport Complex I