The serum-inducible protein kinase Snk is a G1 phase polo-like kinase that is inhibited by the calcium- and integrin-binding protein CIB.

Identified as an immediate-early transcript, the serum-inducible kinase Snk bears sequence homology with the polo-like kinases. Endogenous Snk was detected in early G(1) in NIH 3T3 cells, and nascent Snk showed a half-life of about 15 min. The kinase activity of endogenous Snk was detected in G(1). Substitution of Thr-236 ...
with a glutamate residue increased Snk kinase activity by about 10-fold, whereas substitution of Lys-108 abolished its kinase activity. Disrupting the polo-box did not significantly change Snk kinase activity. A GFP-C-Snk fusion protein showed polo-box-dependent localization to the microtubule organizing center, and ectopic expression of Snk in COS-7 cells induced changes in cell morphology, depending on Snk kinase activity and the polo-box. The capacity of Snk to induce morphological changes was inhibited by the calcium- and integrin-binding protein CIB. CIB co-immunoprecipitated with Snk and inhibited the kinase activity of Snk, suggesting that CIB is a negative regulator for Snk kinase activity.
Mesh Terms:
3T3 Cells, Animals, COS Cells, Calcium-Binding Proteins, Carrier Proteins, Cell Cycle Proteins, Enzyme Activation, G1 Phase, Gene Expression Regulation, Enzymologic, Mice, Precipitin Tests, Protein Kinases, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins
Mol. Cancer Res.
Date: Mar. 01, 2003
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