Characterization of proteins phosphorylated by the cAMP-dependent protein kinase of bovine heart mitochondria

FEBS Lett. 1995 Dec 27;377(3):470-4. doi: 10.1016/0014-5793(95)01407-1.

Abstract

Characterization of two mitochondrial proteins of M(r) 42 and 18 kDa, respectively, phosphorylated by the cAMP-dependent protein kinase of bovine heart mitochondria (mtPKA), is presented. A 42 kDa protein is found to be loosely associated to complexes I, III and IV of the respiratory chain and complex V (ATP synthase) in the inner mitochondrial membrane. An 18 kDa protein is associated to complex I in the inner membrane and in a purified preparation of this complex where it can be phosphorylated by the isolated catalytic subunit of PKA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphate / metabolism
  • Animals
  • Carrier Proteins*
  • Cattle
  • Cyclic AMP-Dependent Protein Kinases / metabolism*
  • Electron Transport Complex IV / metabolism
  • Electrophoresis, Gel, Two-Dimensional
  • Membrane Proteins / metabolism
  • Mitochondria, Heart / enzymology
  • Mitochondria, Heart / metabolism*
  • Mitochondrial Proton-Translocating ATPases
  • NAD(P)H Dehydrogenase (Quinone) / metabolism
  • Phosphoproteins / biosynthesis*
  • Phosphorylation

Substances

  • Carrier Proteins
  • Membrane Proteins
  • Phosphoproteins
  • Adenosine Triphosphate
  • NAD(P)H Dehydrogenase (Quinone)
  • Electron Transport Complex IV
  • Cyclic AMP-Dependent Protein Kinases
  • Adenosine Triphosphatases
  • Mitochondrial Proton-Translocating ATPases
  • oligomycin sensitivity-conferring protein