Kohtz D S, Puszkin S
Laboratory of Molecular Pathology, Mount Sinai School of Medicine, CityUniversity of New York, New York 10029.
J Neurochem. 1989 Jan;52(1):285-95. doi: 10.1111/j.1471-4159.1989.tb10929.x.
We recently described a new protein associated exclusively with neuronal clathrin-coated vesicles (CCVs), and characterized two monoclonal antibodies that react with it (S-8G8 and S-6G7). In this report, the association of neuronal protein of 185 kilodaltons (NP185) with CCV kinases and its interaction with tubulin are described. The affinity of NP185 for tubulin is significantly enhanced when tubulin is phosphorylated by CCV-associated casein kinase II. In contrast, phosphorylation of tubulin by a kinase activity associated with purified brain tubulin decreases its affinity for NP185. Together, these data suggest that the interaction of NP185 with tubulin is modulated by protein phosphorylation. Recent evidence has suggested that tubulin is phosphorylated by casein kinase II during neurite development. The enhanced affinity of NP185 for tubulin phosphorylated by casein kinase II could be important for proper intracellular sorting of this protein in the developing neuron.
我们最近描述了一种仅与神经元网格蛋白包被小泡（CCV）相关的新蛋白质，并鉴定了两种与之反应的单克隆抗体（S-8G8和S-6G7）。在本报告中，描述了185千道尔顿神经元蛋白（NP185）与CCV激酶的关联及其与微管蛋白的相互作用。当微管蛋白被CCV相关的酪蛋白激酶II磷酸化时，NP185对微管蛋白的亲和力显著增强。相反，与纯化的脑微管蛋白相关的激酶活性对微管蛋白的磷酸化会降低其对NP185的亲和力。总之，这些数据表明NP185与微管蛋白的相互作用受蛋白质磷酸化调节。最近的证据表明，在神经突发育过程中，酪蛋白激酶II会使微管蛋白磷酸化。NP185对酪蛋白激酶II磷酸化的微管蛋白的亲和力增强，这对于该蛋白质在发育中的神经元中进行适当的细胞内分选可能很重要。
