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Protein phosphorylation in isolated mitochondria and the effects of protein kinase C
Author(s) -
Backer J.M.,
Arcoleo J.P.,
Weinstein I.B.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80530-0
Subject(s) - phosphorylation , mitochondrion , protein phosphorylation , protein kinase a , autophagy related protein 13 , biochemistry , biology , atp–adp translocase , kinase , cgmp dependent protein kinase , chemistry , microbiology and biotechnology , cyclin dependent kinase 2 , inner mitochondrial membrane
When isolated intact rat liver mitochondria are incubated with [γ‐ 32 P]ATP the major phosphorylated proteins are those of 47 and 36 kDa. Phosphorylation of the 47 kDa protein, but not of the 36 kDa protein, is inhibited by carboxyatractyloside, an inhibitor of mitochondrial ATP uptake, while phosphorylation of the 36 kDa protein is inhibited by various uncouplers and an inhibitor of mitochondrial respiration. Addition of purified protein kinase C to the isolated mitochondria leads to the phosphorylation of 69, 37 and 17 kDa proteins. As with other substrates for protein kinase C, phosphorylation of these proteins is dependent on Ca 2+ and markedly stimulated by various tumor promoters.