细胞质动力蛋白的蛋白质磷酸化增加会导致运动功能受损。
Increased protein phosphorylation of cytoplasmic dynein results in impaired motor function.
作者信息
Runnegar M T, Wei X, Hamm-Alvarez S F
机构信息
Department of Medicine, University of Southern California, 1985 Zonal Avenue, Los Angeles, CA 90089-9121, USA.
出版信息
Biochem J. 1999 Aug 15;342 ( Pt 1)(Pt 1):1-6.
Abstract
Inhibition of serine/threonine protein phosphatases in rat hepatocytes by okadaic acid and microcystin increased the phosphorylation of several components of the cytoplasmic dynein complex. UV light/vanadate cleavage and Western blot analysis revealed that two of these components with molecular masses of approx. 400 kDa and 74 kDa were dynein heavy- and intermediate-chains respectively. This increased phosphorylation resulted in inhibition of dynein ATPase activity, and reduced motor-dependent avidity of endosomal/lysosomal membranes for microtubules.
摘要
冈田酸和微囊藻毒素对大鼠肝细胞中丝氨酸/苏氨酸蛋白磷酸酶的抑制作用增加了胞质动力蛋白复合体几个组分的磷酸化。紫外线/钒酸盐切割和蛋白质印迹分析表明，其中两个分子量分别约为400 kDa和74 kDa的组分分别是动力蛋白重链和中间链。这种磷酸化增加导致动力蛋白ATP酶活性受到抑制，并降低了内体/溶酶体膜对微管的运动依赖性亲和力。
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