cdk5 expression and association with p35nck5a in early stages of rat cerebellum neurogenesis; tyrosine dephosphorylation and activation in post-mitotic neurons

Neurosci Lett. 1996 Oct 25;218(1):21-4. doi: 10.1016/0304-3940(96)13106-2.

Abstract

We have examined the expression of cyclin dependent kinase (cdk) 5 protein kinase and p35nck5a, its activator subunit, during postnatal neurogenesis in rat cerebellum, using mono-specific antibodies. Both cdk5 and p35nck5a are present and associated in proliferative stages, although cdk5-p35 kinase activity is barely detectable. Cdk5-p35 activity, but not the expression of either subunit, increases up to 6-fold during neuronal differentiation. Since we observe that cdk5 is phosphorylated on tyrosine in proliferative, but not in post-mitotic stages, we suggest that post-translational regulatory mechanisms control cdk5-p35 protein kinase activity during neurogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Cerebellum / metabolism*
  • Cyclin-Dependent Kinase 5
  • Cyclin-Dependent Kinases*
  • Immunohistochemistry
  • Mitosis / physiology*
  • Protein Serine-Threonine Kinases / metabolism*
  • Rats
  • Tyrosine / metabolism*

Substances

  • Tyrosine
  • Cyclin-Dependent Kinase 5
  • Protein Serine-Threonine Kinases
  • Cdk5 protein, rat
  • Cyclin-Dependent Kinases