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首页> 美国卫生研究院文献>Cell Regulation >A Novel Role of Nectins in Inhibition of the E-Cadherin–induced Activation of Rac and Formation of Cell-Cell Adherens Junctions
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A Novel Role of Nectins in Inhibition of the E-Cadherin–induced Activation of Rac and Formation of Cell-Cell Adherens Junctions

机译：果胶在抑制E-钙黏着蛋白诱导的Rac活化和细胞-细胞粘附连接的形成中的新作用。

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Nectins are Ca2+-independent immunoglobulin (Ig)-like cell-cell adhesion molecules. The trans-interactions of nectins recruit cadherins to the nectin-based cell-cell adhesion, resulting in formation of cell-cell adherens junctions (AJs) in epithelial cells and fibroblasts. The trans-interaction of E-cadherin induces activation of Rac small G protein, whereas the trans-interactions of nectins induce activation of not only Rac but also Cdc42 small G protein. We showed by the fluorescent resonance energy transfer (FRET) imaging that the trans-interaction of E-cadherin induced dynamic activation and inactivation of Rac, which led to dynamic formation and retraction of lamellipodia. Moreover, we found here that the nectins, which did not trans-interact with other nectins (non–trans-interacting nectins), inhibited the E-cadherin–induced activation of Rac and reduced the velocity of the formation of the E-cadherin-based cell-cell AJs. The inhibitory effect of non–trans-interacting nectins was suppressed by the activation of Cdc42 induced by the trans-interactions of nectins. These results indicate a novel role of nectins in regulation of the E-cadherin–induced activation of Rac and formation of cell-cell AJs.
机译：凝集素是独立于Ca 2 + 的免疫球蛋白（Ig）样细胞间粘附分子。果胶的反式相互作用将钙粘着蛋白募集到基于果胶的细胞间粘附，从而导致上皮细胞和成纤维细胞中细胞间粘附连接（AJ）的形成。 E-钙粘着蛋白的反式相互作用诱导Rac小G蛋白的活化，而果胶的反式相互作用不仅诱导Rac而且Cdc42小G蛋白的活化。我们通过荧光共振能量转移（FRET）成像表明，E-钙粘着蛋白的反式相互作用诱导Rac的动态激活和失活，从而导致片状脂蛋白的动态形成和收缩。此外，我们在这里发现未与其他果胶（非反式相互作用果胶）反式相互作用的果胶抑制了E-钙黏着蛋白诱导的Rac活化并降低了E-钙黏着蛋白的形成速度。基于单元格的AJ。非反式相互作用的果胶的抑制作用被果胶的反式相互作用诱导的Cdc42激活所抑制。这些结果表明，凝集素在调节E-钙粘蛋白诱导的Rac激活和细胞AJs形成中起着新的作用。

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