Cdk5 regulates differentiation of oligodendrocyte precursor cells through the direct phosphorylation of paxillin

• DOI: 10.1242/jcs.018218
• Publication Date: 2007-11-28T01:26:23Z
• Authors: Yuki Miyamoto; Junji Yamauchi; Jonah R. Chan; Atsumasa Okada; Yasuhiro Tomooka; Shin-ichi Hisanaga; Akito Tanoue
• Keywords: Cyclin-dependent kinase 5; Paxillin; PTK2

Oligodendrocyte precursor cells (OPCs) differentiate into oligodendrocytes (OLs) in order to form myelin, which is required for the rapid propagation of action potentials vertebrate nervous system. In spite considerable clinical importance myelination, little known about basic molecular mechanisms underlying OL differentiation and myelination. Here, we show that cyclin-dependent kinase (Cdk) 5 activated following induction differentiation, Cdk5 inhibitor roscovitine inhibits differentiation. The complexity processes also diminished after knocking down endogenous using RNAi. We focal adhesion protein paxillin directly phosphorylated at Ser244 by Cdk5. Transfection a construct harboring Ala mutation dramatically its morphological effects. Importantly, phosphorylation reduces interaction with (FAK). Taken together, these results suggest key mechanism may ultimately regulate