Formation of Kv2.1-FAK complex as a mechanism of FAK activation, cell polarization and enhanced motility.
J Cell Physiol
; 217(2): 544-57, 2008 Nov.
Article
en En
| MEDLINE
| ID: mdl-18615577
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Movimiento Celular
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Corteza Cerebral
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Polaridad Celular
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Quinasa 1 de Adhesión Focal
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Canales de Potasio Shab
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Neuronas
Idioma:
En
Revista:
J Cell Physiol
Año:
2008
Tipo del documento:
Article
País de afiliación:
China
Pais de publicación:
Estados Unidos