Gascard P, Mohandas N
Lawrence Berkeley National Laboratory, Department of Subcellular Structure, California 94720, USA.
Curr Opin Hematol. 2000 Mar;7(2):123-9. doi: 10.1097/00062752-200003000-00009.
This article presents new insights into potential roles that three erythrocyte cytoskeletal proteins, protein 4.1, ankyrin, and spectrin, may play in nonerythroid nucleated cells. Each of these proteins is encoded by several closely related genes characterized by complex alternative splicing of their pre-mRNA, thus resulting in the cellular expression of a broad repertoire of isoforms that can adopt tissue- and cell-specific distribution. This could account for the presence of skeletal networks in intracellular organelles such as lysosomes, the Golgi apparatus, or the nucleus. In addition to providing structural support to cell membranes, these cytoskeletal proteins regulate the functions of various transmembrane proteins they interact with, in particular ion channels, as well as the activity of membrane-bound enzymes. Thus, they appear to be key players in major unsuspected cell functions such as protein sorting, dynamics of nuclear architecture during mitosis, or regulation of signal transduction pathways.
本文介绍了三种红细胞细胞骨架蛋白(蛋白4.1、锚蛋白和血影蛋白)可能在非红细胞有核细胞中发挥的潜在作用的新见解。这些蛋白中的每一种都由几个密切相关的基因编码,其特征是前体mRNA存在复杂的可变剪接,从而导致细胞表达多种亚型,这些亚型可呈现组织和细胞特异性分布。这可以解释细胞内细胞器(如溶酶体、高尔基体或细胞核)中存在骨架网络的原因。除了为细胞膜提供结构支持外,这些细胞骨架蛋白还调节它们与之相互作用的各种跨膜蛋白的功能,特别是离子通道,以及膜结合酶的活性。因此,它们似乎是一些未被充分认识的主要细胞功能(如蛋白质分选、有丝分裂期间核结构的动态变化或信号转导途径的调节)中的关键参与者。