THE PHOSPHORYLATION OF STATHMIN BY MAP KINASE
THE PHOSPHORYLATION OF STATHMIN BY MAP KINASE
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DOI：
10.1007/bf01076766
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发表时间：
1993-11-01
影响因子：
4.3
通讯作者：
SOBEL, A
中科院分区：
文献类型：
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作者：
LEIGHTON, IA;CURMI, P;SOBEL, A
Stathmin是一种普遍存在的胞浆磷蛋白，在细胞增殖、分化和其他细胞功能的调节中起着整合多种信号的作用，在体外可被丝裂原活化蛋白激酶（MAP）快速、化学计量地磷酸化。Ser-25被确定为磷酸化的主要位点，Ser-38为磷酸化的次要位点，而MAP激酶的p42和p44亚型是在神经生长因子（NGF）刺激后在PC 12细胞中检测到的唯一显著的stathmin激酶。结果表明，MAP激酶是负责增加Ser-25磷酸化水平的酶，这在以前的PC 12细胞中观察到的NGF刺激后。
Stathmin, a ubiquitous cytosolic phosphoprotein which may play a role in integrating the effects of diverse signals regulating proliferation, differentiation and other cell functions, was found to be phosphorylated rapidly and stoichiometrically by mitogen-activated protein (MAP) kinase in vitro. Ser-25 was identified as the major site and Ser-38 as a minor site of phosphorylation, while the p42 and p44 isoforms of MAP kinase were the only significant stathmin kinases detected in PC12 cells after stimulation by nerve growth factor (NGF). The results suggest that MAP kinases are the enzymes responsible for increasing the level of phosphorylation of Ser-25, which has been observed previously in PC12 cells following stimulation by NGF.