MAP kinase binds to the NH2‐terminal activation domain of c‐Myc

FEBS Letters

Davis, Roger J.¹  Gupta, Shashi¹ 

[1] Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, and Howard Hughes Medical Institute, 373 Plantation Street, Worcester, MA 01605, USA

关键词: MAP kinase;    c-Myc;    Protein phosphorylation;   

DOI  :  10.1016/0014-5793(94)01052-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown