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

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.

Wei, Ling (författare)
Zhou, Xin (författare)
Lu, Zhong-Yang (författare)
Francis, Kevin (författare)
Hu, Xin-Yang (författare)
Liu, Yu (författare)
Xiong, Wen-Cheng (författare)
Zhang, XiaoUppsala universitet,Institutionen för folkhälso- och vårdvetenskap(Swepub:uu)xiaozhan (författare)
Banik, Naren L. (författare)
Zheng, Shu-Sen (författare)
Yu, Shan Ping (författare)
Uppsala universitetInstitutionen för folkhälso- och vårdvetenskap (creator_code:org_t)

Ingår i:Journal of Cellular Physiology: Wiley217:2, s. 544-5570021-95411097-4652

Av författaren/redakt...: Wei, Jian-Feng; Wei, Ling; Zhou, Xin; Lu, Zhong-Yang; Francis, Kevin; Hu, Xin-Yang; visa fler...; Liu, Yu; Xiong, Wen-Cheng; Zhang, Xiao; Banik, Naren L.; Zheng, Shu-Sen; Yu, Shan Ping; visa färre...

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