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A conserved role for myosin VII in adhesion

机译:肌球蛋白VII在粘附中的守恒作用

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摘要

The class VII myosins (M7) are expressed in a wide range of organisms. M7 mutants in mice, zebrafeh and Dictyostelium exhibit phenotypes that reveal a role for M7 in adhesion in these highly divergent systems, suggesting a basic conservation of M7 function throughout evolution. M7s arc characterized by the presence of two FERM domains in their C-terminal tail region, and deletion of either from the Dictyostelium M7 (DdM7) tail results in Loss of function without affecting localization. A search for DdM7 binding partners has revealed that talin, an actin-binding protein that provides a key link between adhesion receptors and the actin cytoskeleton, interacts directly with DdM7. The phenotypes of the DdM7 and talin null mutants are highly similar, suggesting that these two proteins work co-operatively to maintain cell-cell and cell-surface contact and that this interaction may also be conserved throughout evolution.
机译:VII类肌苷(M7)在各种各样的生物中表达。 M7突变体在小鼠中,Zebrafeh和Dictyostelium表现出表型,所述表型在这些高度发散的系统中揭示了M7在粘附中的作用,表明在整个演变过程中的基本守恒。 M7S弧形的特征在于它们的C末端尾部区域中的两个FERM域,并且从Dictyostelium M7(DDM7)尾部的缺失导致功能丢失而不会影响局部化。寻找DDM7结合伙伴的揭示瞳孔,一种在粘附受体和肌动蛋白细胞骨架之间提供关键环节的肌动蛋白结合蛋白直接与DDM7相互作用。 DDM7和Talin Null突变体的表型高度相似,表明这两种蛋白质合作地用于维持细胞 - 细胞和细胞表面接触,并且该相互作用也可以在整个进化过程中保守。

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