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首页> 外文期刊>Journal of Cellular Physiology >Formation of Kv2.1-FAK complex as a mechanism of FAK activation, cell polarization and enhanced motility.
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Formation of Kv2.1-FAK complex as a mechanism of FAK activation, cell polarization and enhanced motility.

机译:Kv2.1-FAK形成复杂的机制FAK激活,细胞极化和增强的能动性。

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摘要

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.
机译:粘着斑激酶(FAK)中扮演关键角色细胞粘附和迁移。延迟整流钾通道Kv2.1,通过其在n端LD-like图案,阿美与FAK和增强的磷酸化FAK(397)和FAK(576/577)。Kv2.1和观察FAK的分布soma和近端皮质神经元的树突。FAK的表达促进了偏振膜Kv2.1通道的分布。Kv2.1-transfected CHO细胞的形成Kv2.1-FAK复杂的刺激了纤连蛋白/整合素和抑制的K (+)通道阻断剂四乙铵(茶)。磷酸化被shRNA击倒最小化Kv2.1通道的点突变n端,分别和茶。形态学改变Kv2.1击倒或茶,阻碍细胞的迁移活动。治疗体外测试和创伤性损伤动物模型,Kv2.1表达式co-localization Kv2.1 FAK显著增强细胞定向迁移和伤口关闭。可以作为促进FAK信号吗激活,细胞的能动性。

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