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The β-Thymosin Enigma

机译:β-胸腺蛋白

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摘要

Actin dynamics in nonmuscle cells is controlled by the availability of actin nucleating sites and actin monomers. Thymosin β-4 (Tβ-4) has been implicated in modulating the availability of actin monomers in a large variety of cells. It together with actin nucleating, severing, and uncapping proteins, harnesses the intrinsic dynamic properties of actin to regulate the actin polymerization response in cells. Over-expression or addition of exogenous Tβ-4 or its homolog, Tβ-10, alters the actin cytoskeleton, and has multiple effects on cellular functions related to motility. Some of these effects are consistent with β-thymosins functioning exclusively as monomer-binding proteins, while others are not. Therefore, the complex pleiotropic effects of β-thymosin in cells may be due to direct and indirect effects on the actin cytoskeleton, as well as modulation of signaling pathways that will impact the cytoskeleton and a variety of cell functions.
机译:非用途细胞中的肌动蛋白动态由肌动蛋白成核位点和肌动蛋白单体的可用性控制。胸腺蛋白β-4(Tβ-4)涉及调节大量细胞中肌动蛋白单体的可用性。与肌动蛋白成核,切断和未接下来的蛋白质一起,利用肌动蛋白的内在动态性质来调节细胞中的肌动蛋白聚合反应。过度表达或添加外源Tβ-4或其同源物Tβ-10,改变肌动蛋白细胞骨架,并对与运动有关的细胞功能具有多种影响。其中一些效果与β-胸苷一致,其仅作为单体结合蛋白,而其他效果则不一致。因此,β-胸苷蛋白在细胞中的复杂性磷酸效应可能是由于对肌动蛋白细胞骨架的直接和间接影响,以及将影响细胞骨架和各种细胞功能的信号传导途径的调节。

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