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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; et al. (Profiled Author: Wencheng Xiong)
Journal of Cellular Physiology. 2008;217(2):544-557.Abstract
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. © 2008 Wiley-Liss, Inc.
PMID: 18615577 PMCID: PMC2562431
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