杆状末端和尾部在波形蛋白中间丝组装及中间丝网络形成中的作用。
The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
作者信息
McCormick M B, Kouklis P, Syder A, Fuchs E
机构信息
Howard Hughes Medical Institute, Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637.
出版信息
J Cell Biol. 1993 Jul;122(2):395-407. doi: 10.1083/jcb.122.2.395.
Abstract
Using mutagenesis, we investigated the importance of two vimentin domains: (a) a highly conserved segment near the carboxy end of the alpha-helical rod, and (b) the tail, with which the rod end is known to interact. As judged by in vitro filament assembly and expression in transiently transfected cells lacking an endogenous vimentin network, the rod-tail interaction is not essential for 10 nm filament structure in vitro or for formation of fibrous arrays in culture. However, when mutated, amino acid residues within the rod and the tail segments can cause perturbations in IF assembly and in IF network formation. Finally, our studies show that the vimentin tail seems to play a role both in thermodynamically stabilizing IF structure in vitro and in establishing proper IF networks in vivo.
摘要
我们利用诱变技术研究了波形蛋白两个结构域的重要性
(a) α-螺旋杆状结构羧基末端附近的一个高度保守片段，以及(b) 已知与杆状结构末端相互作用的尾部。通过体外丝状组装以及在缺乏内源性波形蛋白网络的瞬时转染细胞中的表达来判断，杆状结构与尾部的相互作用对于体外10 nm丝状结构或培养物中纤维阵列的形成并非必不可少。然而，当杆状结构和尾部片段内的氨基酸残基发生突变时，会导致中间丝组装和中间丝网络形成受到干扰。最后，我们的研究表明，波形蛋白尾部似乎在体外热力学稳定中间丝结构以及在体内建立适当的中间丝网络方面都发挥着作用。
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本文引用的文献
1
Compound helical configurations of polypeptide chains: structure of proteins of the alpha-keratin type.多肽链的复合螺旋构型：α-角蛋白类型蛋白质的结构
Nature. 1953 Jan 10;171(4341):59-61. doi: 10.1038/171059a0.
2
Structural studies on the microfibrillar proteins of wool: characterization of the alpha-helix-rich particle produced by chymotryptic digestion.羊毛微原纤维蛋白的结构研究：胰凝乳蛋白酶消化产生的富含α-螺旋颗粒的表征
Aust J Biol Sci. 1981;34(5-6):515-26. doi: 10.1071/bi9810515.
3
4
Disruption of the in vivo distribution of the intermediate filaments in fibroblasts through the microinjection of a specific monoclonal antibody.通过显微注射特异性单克隆抗体破坏成纤维细胞中间丝的体内分布。
Cell. 1981 Apr;24(1):185-93. doi: 10.1016/0092-8674(81)90514-6.
5
Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments.波形蛋白N端多肽在中间丝形成中的作用。
J Cell Sci. 1983 Sep;63:43-67. doi: 10.1242/jcs.63.1.43.
6
Heterotypic tetramer (A2D2) complexes of non-epidermal keratins isolated from cytoskeletons of rat hepatocytes and hepatoma cells.从大鼠肝细胞和肝癌细胞的细胞骨架中分离出的非表皮角蛋白的异型四聚体（A2D2）复合物。
J Mol Biol. 1984 Sep 15;178(2):365-88. doi: 10.1016/0022-2836(84)90149-9.
7
The number of polypeptide chains in the rod domain of bovine epidermal keratin.牛表皮角蛋白杆状结构域中的多肽链数量。
Biochem Int. 1983 Dec;7(6):769-74.
8
The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins.鸡肌肉结蛋白的氨基酸序列为中间丝蛋白提供了一个通用的结构模型。
EMBO J. 1982;1(12):1649-56. doi: 10.1002/j.1460-2075.1982.tb01368.x.
9
The cDNA sequence of a human epidermal keratin: divergence of sequence but conservation of structure among intermediate filament proteins.人表皮角蛋白的cDNA序列：中间丝蛋白序列存在差异但结构保守
Cell. 1982 Nov;31(1):243-52. doi: 10.1016/0092-8674(82)90424-x.
10
Assembly of vimentin in vitro and its implications concerning the structure of intermediate filaments.波形蛋白的体外组装及其对中间丝结构的影响。
J Mol Biol. 1985 Jun 5;183(3):365-75. doi: 10.1016/0022-2836(85)90007-5.
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