Identification of a novel, membrane-associated neuronal kinase, cyclin-dependent kinase 5/p35-regulated kinase.
Item Type:Journal Article
Citation:Kesavapany, S, Lau, KF, Ackerley, S, Banner, SJ, Shemilt, SJ, Cooper, JD, Leigh, PN, Shaw, CE, McLoughlin, DM, Miller, CC, `Identification of a novel, membrane-associated neuronal kinase, cyclin-dependent kinase 5/p35-regulated kinase? in The Journal of Neuroscience, 23, (12), 2003, pp 4975 - 4983
Identification of a novel, membrane-associated neuronal kinase, cyclin-dependent kinase 5 p35-regulated kinase.pdf (published (publisher copy) peer-reviewed) 479.1Kb
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.
Medical Research Council
Author: MCLOUGHLIN, DECLAN
Publisher:The Society for Neuroscience
Type of material:Journal Article
Series/Report no:The Journal of Neuroscience
Availability:Full text available