Evolution of spectrin function in cytoskeletal and membrane networks
Evolution of spectrin function in cytoskeletal and membrane networks
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DOI：
10.1042/bst0370796
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发表时间：
2009-08-01
影响因子：
3.9
通讯作者：
Baines, Anthony J.
中科院分区：
文献类型：
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作者：
Baines, Anthony J.
幽灵蛋白是一种细胞骨架蛋白，被认为是类似α-肌动蛋白的祖先的后代。它是在动物进化过程中产生的，通过组装信号和细胞黏附复合体、增强膜的机械稳定性和促进特化膜域的组装来促进细胞与组织的整合。血影蛋白的功能是(α-β([H]))(2)四聚体，直接或通过连接蛋白如锚蛋白和4.1将跨膜蛋白、膜脂和肌动蛋白细胞骨架连接起来。在这篇论文中，我回顾了关于这一系统的起源和适应的最新研究结果。(I)短尾有节鞭毛虫的基因组编码α-、β-和β(重)-血影蛋白，表明血影蛋白是在动物的直接单细胞前体中进化的。(Ii)Ankyrin和4.1不在该基因组中编码，这表明在随后的动物进化过程中，血影蛋白获得了功能。(Iii)在脊椎动物的进化中，蛋白质4.1获得了与血影蛋白结合的活性。(Iv)鸡或哺乳动物β-光谱蛋白与PtdInsP(2)的相互作用可以通过差异mRNA剪接来调节，这可以消除βI-或βII-光谱蛋白中的PH(Pleckstrin同源)结构域；对于哺乳动物填充-光谱蛋白，替代的C-末端编码一个调节与α-光谱蛋白相互作用的磷酸化位点。(V)在哺乳动物进化中，复制了单一的预先存在的阿尔法血影蛋白基因，并使其中一对(阿尔法I)具有新的功能化，以实现四聚体的快速成败。我假设哺乳动物非有核红细胞的弹性取决于血影蛋白二聚体/四聚体在循环中所经历的剪切力下的动态重排。
Spectrin is a cytoskeletal protein thought to have descended from an alpha-actinin-like ancestor. It emerged during evolution of animals to promote integration of cells into tissues by assembling signalling and cell adhesion complexes, by enhancing the mechanical stability of membranes and by promoting assembly of specialized membrane domains. spectrin functions as an (alpha beta([H]))(2) tetramer that cross-links transmembrane proteins, membrane lipids and the actin cytoskeleton, either directly or via adaptor proteins such as ankyrin and 4.1. In the present paper, I review recent findings on the origins and adaptations in this system. (i) The genome of the choanoflagellate Monosiga brevicollis encodes alpha-, beta- and beta(Heavy)-spectrin, indicating that spectrins evolved in the immediate unicellular precursors of animals. (ii) Ankyrin and 4.1 are not encoded in that genome, indicating that spectrin gained function during subsequent animal evolution. (iii) Protein 4.1 gained a spectrin-binding activity in the evolution of vertebrates. (iv) interaction of chicken or mammal beta-spectrin with PtdInsP(2) can be regulated by differential mRNA splicing, which can eliminate the PH (pleckstrin homology) domain in beta I- or beta II-spectrins; in the case of mammalian fill-spectrin, the alternative C-terminal region encodes a phosphorylation site that regulates interaction with alpha-spectrin. (v) in mammalian evolution, the single pre-existing alpha-spectrin gene was duplicated, and one of the resulting pair (alpha I) neo-functionalized for rapid make-and-break of tetramers. I hypothesize that the elasticity of mammalian non-nucleated erythrocytes depends on the dynamic rearrangement of spectrin dimers/tetramers under the shearing forces experienced in circulation.