Cyclin-dependent kinase 5 with phosphorylation of tyrosine 15 residue is enriched in striatal matrix compartment in adult mice

R Morigaki; W Sako; S Okita; J Kasahara; H Yokoyama; S Nagahiro; R Kaji; S Goto

doi:10.1016/j.neuroscience.2011.05.055

Cyclin-dependent kinase 5 with phosphorylation of tyrosine 15 residue is enriched in striatal matrix compartment in adult mice

Neuroscience. 2011 Aug 25:189:25-31. doi: 10.1016/j.neuroscience.2011.05.055. Epub 2011 May 31.

Authors

R Morigaki¹, W Sako, S Okita, J Kasahara, H Yokoyama, S Nagahiro, R Kaji, S Goto

Affiliation

¹ Parkinson's Disease and Dystonia Research Center, Tokushima University Hospital, University of Tokushima, Tokushima 770-8503, Japan.

PMID: 21640796
DOI: 10.1016/j.neuroscience.2011.05.055

Abstract

Accumulating evidence suggests that the striosome-matrix systems have a tight link with motor and behavioral brain functions and their disorders. Cyclin-dependent kinase 5 (Cdk5) is a versatile protein kinase that plays a role in synaptic functions and cell survival in adult brain, and its kinase activity is stimulated by phosphorylation at tyrosine 15 residue (pY15). In this study, we used an immunohistochemical method to show differential localization of Cdk5-pY15 in the striatal compartments of adult mice, with a heightened density of Cdk5-pY15 labeling in the matrix relative to the striosomes. Our findings indicate that Cdk5-pY15 can be a new marker for the striatal matrix compartment, and suggest a possible involvement of Cdk5-mediated signaling in compartment-specific neurotransmission and disease pathology in the striatum.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Corpus Striatum / anatomy & histology
Corpus Striatum / metabolism*
Cyclin-Dependent Kinase 5 / metabolism*
Immunohistochemistry
Mice
Phosphorylation
Tyrosine / metabolism*

Substances

Tyrosine
Cyclin-Dependent Kinase 5
Cdk5 protein, mouse