cdk5 modulates β- and δ-catenin/Pin1 interactions in neuronal cells

✍ Scribed by Juan P. Muñoz; Claudia H. Huichalaf; Daniel Orellana; Ricardo B. Maccioni

• Book ID: 102305191
• Publisher: John Wiley and Sons
• Year: 2007
• Tongue: English
• Weight: 273 KB
• Volume: 100
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.21041

✦ Synopsis

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 δ‐catenin. Immunocytochemical studies of δ‐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 β‐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 β‐catenin structure as specific phosphorylation sites for cdk5/p35 complex. Moreover, Pin1, a peptidyl–prolyl isomerase (PPIase) directly bound to both, β‐ and δ‐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 β‐ and δ‐catenin. J. Cell. Biochem. 100: 738–749, 2007. © 2006 Wiley‐Liss, Inc.