丝裂原活化蛋白激酶的对接结构域与底物特异性测定

Docking domains and substrate-specificity determination for MAP kinases.

作者信息

Sharrocks A D, Yang S H, Galanis A

机构信息

School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester, UK M13 9PT.

出版信息

Trends Biochem Sci. 2000 Sep;25(9):448-53. doi: 10.1016/s0968-0004(00)01627-3.

DOI:10.1016/s0968-0004(00)01627-3

PMID:10973059

Abstract

Signalling specificity in eukaryotic cells is maintained by several mechanisms. One mechanism by which mitogen-activated protein (MAP) kinases ensure their specificity of action is by interacting with their substrates through docking domains. These docking domains recruit the kinases to the correct substrates and enhance their fidelity and efficiency of action. Additional specificity determinants in the substrates serve to enhance the specificity of substrate phosphorylation by MAP kinases further.

摘要

真核细胞中的信号特异性通过多种机制得以维持。丝裂原活化蛋白（MAP）激酶确保其作用特异性的一种机制是通过对接结构域与底物相互作用。这些对接结构域将激酶招募到正确的底物上，并提高其作用的保真度和效率。底物中的其他特异性决定因素进一步增强了MAP激酶对底物磷酸化的特异性。