DOMAIN-SPECIFIC AND SEQUENCE-SPECIFIC PHOSPHORYLATION OF VIMENTIN INDUCES DISASSEMBLY OF THE FILAMENT STRUCTURE
DOMAIN-SPECIFIC AND SEQUENCE-SPECIFIC PHOSPHORYLATION OF VIMENTIN INDUCES DISASSEMBLY OF THE FILAMENT STRUCTURE
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DOI：
10.1021/bi00433a035
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发表时间：
1989-04-04
期刊：
影响因子：
2.9
通讯作者：
INAGAKI, M
中科院分区：
文献类型：
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作者：
ANDO, S;TANABE, K;INAGAKI, M
我们报道了camp依赖性蛋白激酶或蛋白激酶C的化学计量磷酸化诱导蛋白蛋白丝的分解[Inagaki， M., Nishi， Y., Nishizawa， K., Matsuyama， M., and Sato， C. (1987) Nature 328, 6490652；Inagaki， M., Gonda， Y., Matsuyama， M., Nishizawa， K., Nishi， Y., and Sato， C.（1988）。化学学报，26(3):571 - 578。在目前的工作中，我们试图确定每个蛋白激酶磷酸化的波形蛋白位点。序列分析表明，Ser-8、Ser-9、Ser-20、Ser-25、Ser-33和Ser-41被蛋白激酶C特异性磷酸化，而Ser-46则被camp依赖性蛋白激酶优先磷酸化。两种激酶均与Ser-6、Ser-24、Ser-38、Ser-50和Ser-65反应。蛋白质C的特异性磷酸化位点大多位于精氨酸的氨基端附近，而camp依赖性蛋白激酶的特异性磷酸化位点位于精氨酸的羧基端附近。磷酸化位点只发生在氨基末端的非α。-螺旋头域，特别是在。词的地区。这些结果为研究蛋白丝磷酸化依赖性解体的分子机制提供了线索。
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments [Inagaki, M., Nishi, Y., Nishizawa, K., Matsuyama, M., and Sato, C. (1987) Nature 328, 6490652; Inagaki, M., Gonda, Y., Matsuyama, M., Nishizawa, K., Nishi, Y., and Sato, C. (1988) J. Biol. Chem. 263, 5970-5978]. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50 and Ser-65. Specific phosphorylation sites for protein C are mostly located close to the amino-terminal side of arginine while those for cAMP-dependent protein kinase are located close to the carboxyl-terminal side of arginine. The phosphorylation sites exclusively occur in the amino-terminal non-.alpha.-helical head domain, particularly at the .beta.-turn region. These results provide clues to the molecular mechanisms of phosphorylation-dependent disassembly of vimentin filaments.