MAP KINASE BINDS TO THE NH2-TERMINAL ACTIVATION DOMAIN OF C-MYC

被引:66
作者
GUPTA, S
DAVIS, RJ
机构
[1] UNIV MASSACHUSETTS,SCH MED,DEPT BIOCHEM & MOLEC BIOL,PROGRAM MOLEC MED,WORCESTER,MA 01605
[2] HOWARD HUGHES MED INST,WORCESTER,MA 01605
关键词
MAP KINASE; C-MYC; PROTEIN PHOSPHORYLATION;
D O I
10.1016/0014-5793(94)01052-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The transcription factor c-Myc is a substrate for phosphorylation by MAP kinases. Here we demonstrate that MAP kinase binds to c-Myc. The NH2-terminal region (residues 1-100) is necessary and sufficient for this interaction. Binding to c-Myc is not dependent on the state of MAP kinase activation. However, the c-Myc/MAP kinase complex is disrupted by ATP. Together, these observations indicate that substrate binding interactions contribute to the specificity of phosphorylation by MAP kinases.
引用
收藏
页码:281 / 285
页数:5
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