Uchida T, Ishiguro K, Ohnuma J, Takamatsu M, Yonekura S, Imahori K
Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan.
FEBS Lett. 1994 Nov 21;355(1):35-40. doi: 10.1016/0014-5793(94)01163-x.
Tau protein kinase II (TPKII) is shown by immunoprecipitation to be a complex composed of two subunits, a catalytic subunit, cdk5, and regulatory subunit, p23. By sequence analysis of p23 cDNA, p23 was found to occupy a region from the 99th amino acid residue to the C-terminus of a novel protein with a molecular weight of 34,000 Da, suggesting that this 34 kDa protein is a precursor of p23 (pre-p23). These findings suggest that p23 results from the processing of the precursor protein, pre-p23. The precursor mRNA was expressed most abundantly in rat brain just before and after birth. Expression of pre-p23, but not of cdk5, mRNA changed, coinciding with the developmental change of TPKII activity, suggesting that its expression controls the phosphorylation of tau by the TPKII/TPKI system in the neonatal brain. p23 appears to be a cdk5 activator in neuronal cells.
通过免疫沉淀法显示,tau蛋白激酶II(TPKII)是一个由两个亚基组成的复合体,一个催化亚基cdk5和一个调节亚基p23。通过对p23 cDNA的序列分析,发现p23占据了一种分子量为34,000 Da的新蛋白质从第99个氨基酸残基到C末端的区域,这表明这种34 kDa的蛋白质是p23的前体(前体p23)。这些发现表明p23是由前体蛋白前体p23加工而来的。前体mRNA在大鼠出生前后在大鼠脑中表达最为丰富。前体p23而非cdk5的mRNA表达发生了变化,这与TPKII活性的发育变化相一致,表明其表达控制了新生脑中TPKII/TPKI系统对tau的磷酸化作用。p23似乎是神经元细胞中的一种cdk5激活剂。