Topology of the mitochondrial cAMP‐dependent protein kinase and its substrates

FEBS Letters

Mazzocca, Antonio¹  Scacco, Salvatore¹  Speranza, Francesco¹  Sardanelli, Anna Maria¹  Technikova-Dobrova, Zuzana²  Papa, Sergio¹ 

[1] Institute of Medical Biochemistry and Chemistry, CNR University of Bari, Bari, Italy;Institute of Microbiology, Czech Academy of Sciences, Praha, Czech Republic

关键词: Mitochondrion;    Protein phosphorylation;    Protein kinase;    Cyclic AMP;    Cyclic AMP-dependent protein kinase;    PMSF;    phenylmethylsulfonil fluoride;    PAGE;    polyacrylamide gel-electrophoresis;    SDS;    sodium dodecylsulphate;    mtPKA;    mitochondrial cAMP-dependent protein kinase;    C-cPKA;    catalitic subunit of purified PKA;   

DOI  :  10.1016/0014-5793(96)01112-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown