Phosphorylation of neurofilament proteins by protein kinase C.
Phosphorylation of neurofilament proteins by protein kinase C.
复制标题
蛋白激酶 C 磷酸化神经丝蛋白。
DOI：
10.1016/0014-5793(88)81380-2
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发表时间：
1988
期刊：
影响因子：
3.5
通讯作者：
Nixon,RA
中科院分区：
文献类型：
--
作者：
Sihag,RK;Jeng,AY;Nixon,RA
神经丝（NF-L）的低分子量（70 kDa）亚基在体内含有至少三个磷酸化位点，并且以位点特异性方式被多种激酶磷酸化[（1987）J. Neurochem. 48，S101; Sihag，R.K.和尼克松，R.A.提交]。在这项研究中，我们观察到，从视网膜神经节细胞神经元的神经丝蛋白的三个亚基是纯化的小鼠脑蛋白激酶C的底物。NF-L亚基的二维α-胰凝乳蛋白酶磷酸肽图谱分析表明，蛋白激酶C磷酸化四个多肽位点，其中两个在体内用[32 P]正磷酸脉冲放射性标记视网膜神经节细胞时掺入磷酸盐。
The low molecular mass (70 kDa) subunit of neurofilaments (NF-L) contains at least three phosphorylation sites in vivo and is phosphorylated by multiple kinases in a site-specific manner [(1987) J. Neurochem. 48, S101; Sihag, R.K. and Nixon, R.A. submitted]. In this study, we observed that the three subunits of neurofilament proteins from retinal ganglion cell neurons are substrates for purified mouse brain protein kinase C. Two-dimensional α-chymotryptic phosphopeptide map analyses of the NF-L subunit demonstrated that protein kinase C phosphorylates four polypeptide sites, two of which incorporate phosphate when retinal ganglion cells are pulse-radiolabeled with [32P]orthophosphate in vivo.