Qi Z, Tang D, Matsuura I, Lee K Y, Zhu X, Huang Q Q, Wang J H
Department of Medical Biochemistry, University of Calgary, Alberta, Canada.
Mol Cell Biochem. 1995 Aug-Sep;149-150:35-9. doi: 10.1007/BF01076561.
Neuronal cdc2-like kinase, nclk, is a heterodimer of cyclin dependent protein kinase 5, cdk5, and a 25 kDa subunit derived from a novel, neuron-specific, 35 kDa protein: p35. The characterization and regulation of nclk will be summarized in this minireview. The activity of nclk appears to be governed by highly complex regulatory mechanisms including protein-protein interaction, protein phosphorylation and isoforms. The histone H1 kinase activity of nclk is absolutely dependent of the interaction between the 25 kDa subunit and the catalytic subunit, cdk5. In addition, nclk interacts with other cellular proteins to form macromolecular complexes. The kinase activity of nclk is inhibited in vitro by the phosphorylation reactions of a weel-like protein tyrosine kinase and a protein serine/threonine kinase from bovine thymus. Northern blot analysis has revealed the existence of two populations of p35 mRNA of 2 and 4 kb. A novel cDNA encoding a p35 homologous protein has been obtained from a human hippocampus library.
神经元细胞周期蛋白依赖性激酶样激酶（nclk）是细胞周期蛋白依赖性蛋白激酶5（cdk5）与一个源自一种新的、神经元特异性的35 kDa蛋白（p35）的25 kDa亚基组成的异二聚体。本综述将总结nclk的特性和调控。nclk的活性似乎受包括蛋白质-蛋白质相互作用、蛋白质磷酸化和同工型在内的高度复杂的调控机制支配。nclk的组蛋白H1激酶活性绝对依赖于25 kDa亚基与催化亚基cdk5之间的相互作用。此外，nclk与其他细胞蛋白相互作用形成大分子复合物。nclk的激酶活性在体外被一种类wee1蛋白酪氨酸激酶和来自牛胸腺的一种蛋白丝氨酸/苏氨酸激酶的磷酸化反应所抑制。Northern印迹分析揭示了存在两种大小分别为2 kb和4 kb的p35 mRNA群体。已从人海马体文库中获得了一个编码p35同源蛋白的新cDNA。
