α-Chimaerin exists in a functional complex with the Cdk5 kinase in brain

• Published in: FEBS letters 2004-03, Vol.561 (1), p.177-180
• Main Authors: Qi, Robert Z, Ching, Yick-Pang, Kung, Hsiang-Fu, Wang, Jerry H
• Format: Article
• Language: English
• Subjects: Brain - enzymology; Cdk, cyclin-dependent kinase; Cdk5; Cdk5 activator; Chimaerin; Chimerin 1 - analysis; Chimerin 1 - genetics; Chimerin 1 - metabolism; Cyclin-Dependent Kinase 5; Cyclin-Dependent Kinases - analysis; Cyclin-Dependent Kinases - genetics; Cyclin-Dependent Kinases - metabolism; Cytoskeleton - metabolism; DTT, dithiothreitol; Gene Library; GSH, glutathione; GST, glutathione S-transferase; HeLa Cells; Humans; Neurons; PBS, phosphate-buffered saline; Precipitin Tests; Protein Binding; Protein–protein interaction; SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis; Transfection; Two-Hybrid System Techniques
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(04)00174-7

Cyclin-dependent kinase 5 (Cdk5) in association with its neuronal activators p35 and p39 shows a complex involvement in the control of neurocytoskeletal dynamics. Here we show that α-chimaerin, a GTPase-activating protein specific for Rac and Cdc42, is a p35-binding protein. The interaction domains of p35 and α-chimaerin were delineated. In transfected HeLa cells, p35 and α-chimaerin displayed an overlapping distribution pattern and they could be co-immunoprecipitated from the cell lysate. As α-chimaerin has a regulatory function in actin repolymerization, these results suggested that the regulation of neurocytoskeleton dynamics by Cdk5 is mediated at least in part via α-chimaerin.