1. GAK: a cyclin G associated kinase contains a tensin/auxilin-like domain.
- Author
-
Kanaoka Y, Kimura SH, Okazaki I, Ikeda M, and Nojima H
- Subjects
- Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Antibodies, Monoclonal, Blotting, Western, Cloning, Molecular, Cyclin G, Cyclin G1, Cyclin-Dependent Kinases metabolism, Cyclins chemistry, Cyclins genetics, DNA, Complementary genetics, Kinetics, Microfilament Proteins chemistry, Molecular Sequence Data, Nerve Tissue Proteins chemistry, Phosphoproteins chemistry, Precipitin Tests, Protein Serine-Threonine Kinases chemistry, Protein Serine-Threonine Kinases genetics, Recombinant Fusion Proteins metabolism, Tensins, Cyclins metabolism, Protein Serine-Threonine Kinases metabolism
- Abstract
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 G-associated kinase). 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.
- Published
- 1997
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