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The Journal of Neuroscience, June 15, 2003, 23(12):4975-4983

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Identification of a Novel, Membrane-Associated Neuronal Kinase, Cyclin-Dependent Kinase 5/p35-Regulated Kinase

Sashi Kesavapany, * Kwok-Fai Lau, * Steven Ackerley, Steven J. Banner, Stephen J. A. Shemilt, Jonathan D. Cooper, P. Nigel Leigh, Christopher E. Shaw, Declan M. McLoughlin, and Christopher C. J. Miller

Departments of Neuroscience and Neurology, The Institute of Psychiatry, Kings College London, London SE5 8AF, United Kingdom

Here we characterize a novel neuronal kinase, cyclin-dependent kinase 5 (cdk5)/p35-regulated kinase (cprk). Cprk is a member of a previously undescribed family of kinases that are predicted to contain two N-terminal membrane-spanning domains and a long C terminus, which harbors a dual-specificity serine/threonine/tyrosine kinase domain. Cprk was isolated in a yeast two-hybrid screen using the neuronal cdk5 activator p35 as "bait." Cprk interacts with p35 in the yeast-two hybrid system, binds to p35 in glutathione S-transferase fusion pull-down assays, and colocalizes with p35 in cultured neurons and transfected cells. In these cells, cprk is present with p35 in the Golgi apparatus. Cprk is expressed in a number of tissues but is enriched in brain and muscle and within the brain is found in a wide range of neuronal populations. Cprk displays catalytic activity in in vitro kinase assays and is itself phosphorylated by cdk5/p35. Cdk5/p35 inhibits cprk activity. Cdk5/p35 may therefore regulate cprk function in the brain.

Key words: cdk5; p35; tau; neurofilament; Alzheimer's disease; amyotrophic lateral sclerosis

Received Oct. 11, 2002; revised Mar. 21, 2003; accepted Mar. 21, 2003.




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