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, Christopher C.J. Miller

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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.

Original languageEnglish
Pages (from-to)4975-4983
Number of pages9
JournalJournal of Neuroscience
Issue number12
StatePublished - Jun 15 2003


  • Alzheimer's disease
  • Amyotrophic lateral sclerosis
  • Cdk5
  • Neurofilament
  • P35
  • Tau


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