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Formation of Kv2.1-FAK complex as a mechanism of FAK activation, cell polarization and enhanced motility.

Jian-Feng Wei, Ling Wei, Xin Zhou, Zhong-Yang Lu, Kevin Francis, Xin-Yang Hu, Yu Liu, Wen-Cheng Xiong, Xiao Zhang, Naren L Banik, Shu-Sen Zheng, Shan Ping Yu

J. Cell. Physiol., 2008 Nov , 217, 544-57

Focal adhesion kinase (FAK) plays key roles in cell adhesion and migration. We now report that the delayed rectifier Kv2.1 potassium channel, through its LD-like motif in N-terminus, may interact with FAK and enhance phosphorylation of FAK(397) and FAK(576/577). Overlapping distribution of Kv2.1 and FAK was observed on soma and proximal dendrites of cortical neurons. FAK expression promotes a polarized membrane distribution of the Kv2.1 channel. In Kv2.1-transfected CHO cells, formation of the Kv2.1-FAK complex was stimulated by fibronectin/integrin and inhibited by the K(+) channel blocker tetraethylammonium (TEA). FAK phosphorylation was minimized by shRNA knockdown of the Kv2.1 channel, point mutations of the N-terminus, and TEA, respectively. Cell migration morphology was altered by Kv2.1 knockdown or TEA, hindering cell migration activity. In wound healing tests in vitro and a traumatic injury animal model, Kv2.1 expression and co-localization of Kv2.1 and FAK significantly enhanced directional cell migration and wound closure. It is suggested that the Kv2.1 channel may function as a promoting signal for FAK activation and cell motility.

http://www.ncbi.nlm.nih.gov/pubmed/18615577