Wilsbacher J L, Goldsmith E J, Cobb M H
Department of Pharmacology, The University of Texas Southwestern Medical Center, Dallas, Texas 75235-9041, USA.
J Biol Chem. 1999 Jun 11;274(24):16988-94. doi: 10.1074/jbc.274.24.16988.
Mitogen-activated protein (MAP) kinases are activated with great specificity by MAP/ERK kinases (MEKs). The basis for the specific activation is not understood. In this study chimeras composed of two MAP kinases, extracellular signal-regulated protein kinase 2 and p38, were assayed in vitro for phosphorylation and activation by different MEK isoforms to probe the requirements for productive interaction of MAP kinases with MEKs. Experimental results and modeling support the conclusion that the specificity of MEK/MAP kinase phosphorylation results from multiple contacts, including surfaces in both the N- and C-terminal domains.
丝裂原活化蛋白（MAP）激酶由MAP/ERK激酶（MEK）以高度特异性激活。这种特异性激活的基础尚不清楚。在本研究中，由两种MAP激酶，即细胞外信号调节蛋白激酶2和p38组成的嵌合体在体外检测了不同MEK同工型的磷酸化和激活情况，以探究MAP激酶与MEK进行有效相互作用的要求。实验结果和模型支持这样的结论，即MEK/MAP激酶磷酸化的特异性源于多个接触点，包括N端和C端结构域中的表面。
