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首页> 外文期刊>European Journal of Cell Biology: Journal of Deutsche Gesellschaft fur Elektronenmikroskopie: Journal of Deutsche Gesellschaft fur Zellbiologie >Tropomyosin assembly intermediates in the control of microfilament system turnover.
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Tropomyosin assembly intermediates in the control of microfilament system turnover.

机译：肌球蛋白组装中间体可控制微丝系统的周转。

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摘要

Tropomyosin is a coiled-coil alpha-helical protein, which self-associates in a head-to-tail fashion along polymers of actin to produce thin filaments. Mammalian non-muscle cells express a large number of tropomyosin isoforms, which are differentially regulated during embryogenesis and associated with specialized actin microfilament ensembles in cells. The function of tropomyosin in specifying form and localization of these subcellular structures, and the precise mechanism(s) by which they carry out their functions, is unclear. This paper reports that, while the major fraction of non-muscle cell tropomyosin resides in actin thin filaments of the cytomatrix, the soluble part of the cytoplasm contains tropomyosins in the form of actin-free multimers, which are isoform specific and of high molecular weight (MW(app) 180,000-250,000). Stimulation of motile cells with growth factors induces a rapid, actin polymerization-dependent outgrowth of lamellipodia and filopodia. Concomitantly, the levels of tropomyosin isoform-specific multimers decrease, suggesting their involvement in actin thin filament formation. Malignant tumor cells have drastically altered levels and composition of tropomyosin isoform-specific multimers as well as tropomyosin in the cytomatrix.
机译：Tropomyosin是一种卷曲螺旋α-螺旋蛋白，它以自始至终的方式与肌动蛋白的聚合物自缔合，从而产生细丝。哺乳动物非肌肉细胞表达大量原肌球蛋白同工型，它们在胚胎发生过程中受到不同的调节，并与细胞中特定的肌动蛋白微丝集合相关。原肌球蛋白在指定这些亚细胞结构的形式和位置中的功能，以及它们执行功能的确切机制尚不清楚。本文报道，尽管非肌肉细胞原肌球蛋白的大部分位于细胞基质的肌动蛋白细丝中，但细胞质的可溶性部分含有原肌球蛋白，其形式为无肌动蛋白的多聚体，具有异构体特异性和高分子量。 （MW（app）180,000-250,000）。用生长因子刺激运动细胞诱导快速的，肌动蛋白聚合反应依赖性的lamellipodia和filopodia的生长。同时，原肌球蛋白同工型特异性多聚体的水平降低，表明它们参与了肌动蛋白细丝的形成。恶性肿瘤细胞的细胞基质中原肌球蛋白同工型特异性多聚体以及原肌球蛋白的水平和组成发生了巨大变化。

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