SITE-SPECIFIC PHOSPHORYLATION INDUCES DISASSEMBLY OF VIMENTIN FILAMENTS INVITRO
SITE-SPECIFIC PHOSPHORYLATION INDUCES DISASSEMBLY OF VIMENTIN FILAMENTS INVITRO
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DOI：
10.1038/328649a0
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发表时间：
1987-08-13
期刊：
影响因子：
64.8
通讯作者：
SATO, C
中科院分区：
文献类型：
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作者：
INAGAKI, M;NISHI, Y;SATO, C
中间丝是真核细胞骨架的主要组成部分。虽然这些纤维至少有五种不同的种类，但间充质起源的细胞和大多数培养细胞含有由亚基蛋白vimentin1组成的中间纤维。Vimentin以非磷酸化和磷酸化的形式存在1 - 4，当丝在各种细胞中经历显著的重新分配时，该蛋白的磷酸化增加5 - 8。磷酸化在静脉蛋白丝的组装-拆卸和组织中的作用仍然不清楚。我们在这里报告了一个稳定和纯化的系统，允许生化检查波形蛋白细丝的组装和拆卸。利用这种体外系统，我们使用纯化的蛋白激酶进行了化学计量磷酸化。我们获得了位点特异性、磷酸化依赖性的波形蛋白细丝分解的证据。
Intermediate filaments are a major component of the cytoskeleton of eukaryotic cells. Although there appear to be at least five distinct classes of these filaments, cells of mesenchymal origin and most cells in culture contain the intermediate filament composed of the subunit protein vimentin1. Vimentin exists in a nonphosphorylated as well as in a phosphorylated form1–4, and there is increased phosphorylation of this protein when the filament undergoes marked redistribution in various cells5–8. The role of phosphoryla-tion on assembly–disassembly and organization of the vimentin filament has remained obscure. We report here a stable and purified system allowing biochemical examination of vimentin filament assembly and disassembly. Using thisin vitrosystem, we carried out stoichiometrical phosphorylations, using purified protein kinases. We obtained evidence for site-specific, phosphorylation-dependent disassembly of the vimentin filament.