Di Paolo G, Antonsson B, Kassel D, Riederer B M, Grenningloh G
Institut de Biologie Cellulaire et de Morphologie, University of Lausanne, Switzerland.
FEBS Lett. 1997 Oct 20;416(2):149-52. doi: 10.1016/s0014-5793(97)01188-5.
Stathmin is a regulator of microtubule dynamics which undergoes extensive phosphorylation during the cell cycle as well as in response to various extracellular factors. Four serine residues are targets for protein kinases: Ser-25 and Ser-38 for proline-directed kinases such as mitogen-activated protein kinase and cyclin-dependent protein kinase, and Ser-16 and Ser-63 for cAMP-dependent protein kinase. We studied the effect of phosphorylation on the microtubule-destabilizing activity of stathmin and on its interaction with tubulin in vitro. We show that triple phosphorylation on Ser-16, Ser-25, and Ser-38 efficiently inhibits its activity and prevents its binding to tubulin.
Stathmin是微管动力学的调节因子，在细胞周期以及对各种细胞外因子的反应过程中会发生广泛的磷酸化。四个丝氨酸残基是蛋白激酶的作用靶点：脯氨酸定向激酶（如丝裂原活化蛋白激酶和细胞周期蛋白依赖性蛋白激酶）作用于Ser-25和Ser-38，而cAMP依赖性蛋白激酶作用于Ser-16和Ser-63。我们在体外研究了磷酸化对Stathmin微管去稳定活性及其与微管蛋白相互作用的影响。我们发现，Ser-16、Ser-25和Ser-38上的三重磷酸化有效地抑制了其活性，并阻止其与微管蛋白结合。
