cdk5 modulates beta- and delta-catenin/Pin1 interactions in neuronal cells.

Abstract:

:The cdk5/p35 complex has been implicated in a variety of functions related to brain development, including axonal outgrown and neuronal migration. In this study, by co-immunoprecipitation and pull-down experiments, we have shown that the cdk5/p35 complex associates with and phosphorylates the neuronal delta-catenin. Immunocytochemical studies of delta-catenin and the cdk5-activator p35 in primary cortical neurons indicated that these proteins co-localize in the cell body of neuronal cells. In addition, cdk5 co-localized with beta-catenin in the cell-cell contacts and plasma membrane of undifferentiated and differentiated N2A cells. In this context, we identified Ser(191) and Ser(246) on beta-catenin structure as specific phosphorylation sites for cdk5/p35 complex. Moreover, Pin1, a peptidyl-prolyl isomerase (PPIase) directly bound to both, beta- and delta-catenin, once they have been phosphorylated by the cdk5/p35 complex. Studies indicate that the cdk5/p35 protein kinase system is directly involved in the regulatory mechanisms of neuronal beta- and delta-catenin.

journal_name

J Cell Biochem

authors

Muñoz JP,Huichalaf CH,Orellana D,Maccioni RB

doi

10.1002/jcb.21041

subject

Has Abstract

pub_date

2007-02-15 00:00:00

pages

738-49

issue

3

eissn

0730-2312

issn

1097-4644

journal_volume

100

pub_type

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