Inada H, Goto H, Tanabe K, Nishi Y, Kaibuchi K, Inagaki M
Laboratory of Biochemistry, Aichi Cancer Center Research Institute, Japan.
Biochem Biophys Res Commun. 1998 Dec 9;253(1):21-5. doi: 10.1006/bbrc.1998.9732.
We obtained evidence that Rho-associated kinase (Rho-kinase) phosphorylates desmin, the myogenic intermediate filament protein, with approximately 2 mol phosphate per mole of desmin in vitro. Desmin phosphorylated by Rho-kinase lost the potential to form 10-nm filaments. Thr-16, Thr-75, and Thr-76 on desmin proved to be the major phosphorylation sites for Rho-kinase. All these sites are located within the head domain and are different from the reported phosphorylation sites of protein kinase. A, protein kinase C, and cdc2 kinase. We are entertaining the notion that Rho-kinase may regulate filament structures of desmin by site-specific phosphorylation.
我们获得的证据表明，在体外，Rho相关激酶（Rho激酶）可使生肌中间丝蛋白结蛋白磷酸化，每摩尔结蛋白约有2摩尔磷酸基团。被Rho激酶磷酸化的结蛋白失去了形成10纳米细丝的能力。结蛋白上的苏氨酸-16、苏氨酸-75和苏氨酸-76被证明是Rho激酶的主要磷酸化位点。所有这些位点都位于头部结构域内，且不同于已报道的蛋白激酶A、蛋白激酶C和细胞周期蛋白依赖性激酶2的磷酸化位点。我们正在考虑这样一种观点，即Rho激酶可能通过位点特异性磷酸化来调节结蛋白的细丝结构。
