Premium
GAK: a cyclin G associated kinase contains a tensin/auxilin‐like domain 1
Author(s) -
Kanaoka Yoshihide,
Kimura Shinya H,
Okazaki Issey,
Ikeda Masako,
Nojima Hiroshi
Publication year - 1997
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(96)01484-6
Subject(s) - microbiology and biotechnology , cyclin dependent kinase complex , cyclin d , cyclin dependent kinase , cyclin , cyclin a2 , cyclin a , immunoprecipitation , kinase , biology , chemistry , cyclin dependent kinase 2 , biochemistry , protein kinase a , cell cycle , gene
We have cloned a cDNA encoding a novel association partner of cyclin G by West‐Western blotting. The cDNA encodes a protein that harbors a Ser/Thr protein kinase‐like catalytic domain at the N‐terminal. Hence, we named it GAK (cyclin ‐ ssociated inase). The long C‐terminal extension shares homology with tensin and auxilin, and contains a leucine zipper region. Co‐immunoprecipitation and Western blotting showed that GAK and cyclin G associate together in vivo. GAK also co‐precipitated with CDK5, and CDK5 was found to be associated with cyclin G. We also showed by BIAcore analysis that the GAK‐cyclin G interaction was direct.