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Formation of Kv2.1-FAK complex as a mechanism of FAK activation, cell polarization and enhanced motility
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2008 (English)In: Journal of Cellular Physiology, ISSN 0021-9541, Vol. 217, no 2, 544-557 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2008. Vol. 217, no 2, 544-557 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-107862DOI: 10.1002/jcp.21530ISI: 000259721800028OAI: oai:DiVA.org:uu-107862DiVA: diva2:233349
Available from: 2009-08-31 Created: 2009-08-31 Last updated: 2009-09-01Bibliographically approved

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