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Topology of the mitochondrial cAMP‐dependent protein kinase and its substrates
Author(s) -
Sardanelli Anna Maria,
Technikova-Dobrova Zuzana,
Speranza Francesco,
Mazzocca Antonio,
Scacco Salvatore,
Papa Sergio
Publication year - 1996
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(96)01112-x
Subject(s) - cytosol , protein kinase a , protein subunit , mitochondrion , inner mitochondrial membrane , microbiology and biotechnology , mitochondrial matrix , phosphorylation , biochemistry , atp–adp translocase , protein phosphorylation , biology , chemistry , enzyme , gene
In intact bovine heart mitochondria, cAMP‐dependent phosphorylation of 42, 29, 18 and 6.5 kDa proteins was inhibited by carboxyatractyloside. This shows that both mitochondrial cAMP‐dependent protein kinase (mtPKA) and its protein substrates are localized at the matrix side of the inner mitochondrial membrane. Proteins of 42, 29, 18, and 6.5 kDa were also bound at the outer surface of mitochondria where they were phosphorylated by the added purified catalytic subunit of PKA. In the cytosol from bovine heart proteins of the above molecular weights were phosphorylated by the cytosolic PKA.