钙调蛋白与细胞骨架功能的调节
Caldesmon and the regulation of cytoskeletal functions.
作者信息
Wang C L Albert
机构信息
Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
出版信息
Adv Exp Med Biol. 2008;644:250-72. doi: 10.1007/978-0-387-85766-4_19.
Abstract
Caldesmon (CaD) is an extraordinary actin-binding protein, because in addition to actin, it also bindsmyosin, calmodulin and tropomyosin. As a component of the smoothmuscle and nonmuscle contractile apparatus CaD inhibits the actomyosin ATPase activity and its inhibitory action is modulated by both Ca2+ and phosphorylation. The multiplicity of binding partners and diverse biochemical properties suggest CaD is a potent and versatile regulatory protein both in contractility and cell motility. However, after decades ofinvestigation in numerous laboratories, hard evidence is still lacking to unequivocally identify its in vivo functions, although indirect evidence is mounting to support an important role in connection with the actin cytoskeleton. This chapter reviews the highlights of the past findings and summarizes the current views on this protein, with emphasis of its interaction with tropomyosin.
摘要
钙调蛋白（CaD）是一种特殊的肌动蛋白结合蛋白，因为除了肌动蛋白外，它还能结合肌球蛋白、钙调蛋白和原肌球蛋白。作为平滑肌和非肌肉收缩装置的组成部分，CaD抑制肌动球蛋白ATP酶活性，其抑制作用受Ca2+和磷酸化的调节。结合伙伴的多样性和多样的生化特性表明，CaD在收缩性和细胞运动性方面都是一种强大且多功能的调节蛋白。然而，经过众多实验室数十年的研究，尽管越来越多的间接证据支持其在肌动蛋白细胞骨架方面发挥重要作用，但仍缺乏确凿证据来明确确定其体内功能。本章回顾了过去研究结果的要点，并总结了关于该蛋白的当前观点，重点是其与原肌球蛋白的相互作用。
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