J. Otto
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引用次数: 35

摘要

Vinculin显然是将细胞相互连接或与底物连接的跨膜组合中的关键元素。然而,尽管对这种蛋白质进行了所有的研究,我们仍然不知道它在这些组合中的功能。大部分生物化学和细胞生物学证据表明,以某种未知的方式,其在连接处的存在可能与肌动蛋白与膜的稳定结合有关,但长春花蛋白本身似乎并不与肌动蛋白相互作用。未来,识别连接肌动蛋白和长春花蛋白的额外连接分子可能会解决这一难题。或者,对磷酸化或酰化的长春花蛋白的研究可能会为其功能提供线索。也许含有微丝连接的蛋白质组成的复杂性表明,蛋白质组合而不是单个蛋白质提供了新的功能。随着属于这些连接的新蛋白质的发现,评估它们与已知成分(如长春花蛋白)的相互作用并询问蛋白质组合是否具有特定功能将是重要的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Vinculin.
Vinculin is clearly a key element in the transmembrane assemblages that link cells to each other or to the substrate. However, despite all the studies that have been done on the protein, we still do not know its function within these assemblages. The bulk of the biochemical and cell biological evidence suggests that, in some unknown way, its presence in the junctions may be involved in the stable association of actin with the membrane, yet vinculin by itself does not appear to interact with actin. In the future, identification of additional junctional molecules that interconnect actin and vinculin may resolve this dilemma. Alternatively, studies with vinculin that is phosphorylated or acylated may yield clues to its function. Perhaps the complexity of the protein composition of microfilament-containing junctions suggests that protein assemblages rather than individual proteins provide novel functions. As new proteins belonging to these junctions are discovered, it will be important to assess their interaction with already known components such as vinculin and to ask if the protein combination has a particular function.
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