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肌动蛋白的非肌肉功能:更新。

The non-muscle functions of actinins: an update.

机构信息

*School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland.

出版信息

Biochem J. 2014 Apr 1;459(1):1-13. doi: 10.1042/BJ20131511.

DOI:10.1042/BJ20131511
PMID:24627985
Abstract

α-Actinins are a major class of actin filament cross-linking proteins expressed in virtually all cells. In muscle, actinins cross-link thin filaments from adjacent sarcomeres. In non-muscle cells, different actinin isoforms play analogous roles in cross-linking actin filaments and anchoring them to structures such as cell-cell and cell-matrix junctions. Although actinins have long been known to play roles in cytokinesis, cell adhesion and cell migration, recent studies have provided further mechanistic insights into these functions. Roles for actinins in synaptic plasticity and membrane trafficking events have emerged more recently, as has a 'non-canonical' function for actinins in transcriptional regulation in the nucleus. In the present paper we review recent advances in our understanding of these diverse cell biological functions of actinins in non-muscle cells, as well as their roles in cancer and in genetic disorders affecting platelet and kidney physiology. We also make two proposals with regard to the actinin nomenclature. First, we argue that naming actinin isoforms according to their expression patterns is problematic and we suggest a more precise nomenclature system. Secondly, we suggest that the α in α-actinin is superfluous and can be omitted.

摘要

α-肌动蛋白是一种主要的肌动蛋白丝交联蛋白,几乎存在于所有细胞中。在肌肉中,肌动蛋白将相邻肌节的细肌丝交联。在非肌肉细胞中,不同的肌动蛋白同工型在交联肌动蛋白丝和将它们锚定到细胞-细胞和细胞-基质连接等结构中发挥类似的作用。尽管肌动蛋白早已被认为在胞质分裂、细胞黏附和细胞迁移中发挥作用,但最近的研究为这些功能提供了进一步的机制见解。肌动蛋白在突触可塑性和膜运输事件中的作用最近也得到了证实,同时,肌动蛋白在核转录调控中的“非典型”功能也得到了证实。本文综述了我们最近对非肌肉细胞中肌动蛋白的这些不同细胞生物学功能的理解进展,以及它们在癌症和影响血小板和肾脏生理学的遗传疾病中的作用。我们还对肌动蛋白命名提出了两个建议。首先,我们认为根据表达模式命名肌动蛋白同工型存在问题,我们建议采用更精确的命名系统。其次,我们建议将α-肌动蛋白中的α删除。

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