Premium
cAMP‐dependent protein kinase and phosphoproteins in mammalian mitochondria. An extension of the cAMP‐mediated intracellular signal transduction
Author(s) -
Papa Sergio,
Sardanelli Anna Maria,
Scacco Salvatore,
Technikova-Dobrova Zuzana
Publication year - 1999
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/s0014-5793(99)00070-8
Subject(s) - protein kinase a , phosphorylation , microbiology and biotechnology , protein phosphorylation , mitochondrion , inner mitochondrial membrane , biology , phosphorylation cascade , inner membrane , protein subunit , signal transduction , cgmp dependent protein kinase , biochemistry , mitogen activated protein kinase kinase , gene
Evidence has been obtained for the occurrence of a cAMP‐dependent serine protein kinase associated with the inner membrane/matrix of mammalian mitochondria. The catalytic site of this kinase is localized at the inner side of the inner membrane, where it phosphorylates a number of mitochondrial proteins. One of these has been identified as the AQDQ subunit of complex I. cAMP‐dependent phosphorylation of this protein promotes the activity of complex I and mitochondrial respiration. A 5 bp duplication in the nuclear gene encoding this protein has been found in a human patient, which eliminates the phosphorylation site. PKA anchoring proteins have recently been identified in the outer membrane of mammalian mitochondria, which could direct phosphorylation of proteins at contact sites with other cell structures.