c-Raf kinase binds to N-terminal domain of c-Myc

被引：4

作者：

Alexandrov, I

Shlyakhova, L

Vartanian, A

Zajac-Kaye, M

Alexandrova, N

机构：

[1] RUSSIAN ACAD SCI, ENGELGARDT INST MOL BIOL, MOSCOW 117984, RUSSIA

[2] RUSSIAN ACAD MED SCI, MENTAL HLTH RES CTR, MOSCOW 113152, RUSSIA

[3] NCI, NAVY ONCOL BRANCH, BETHESDA, MD 20889 USA

来源：

FEBS LETTERS | 1997年 / 414卷 / 02期

基金：

美国国家卫生研究院;

关键词：

c-Raf; c-Myc; protein phosphorylation; protein-protein interaction;

D O I：

10.1016/S0014-5793(97)00992-7

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：

We have demonstrated that the 50 N-terminal amino acids of c-Myc bind a kinase activity, which phosphorylates Myc in vitro predominantly on Thr(8). We also have shown that c-Raf, a widely known Ser/Thr kinase, involved in the Ras signaling pathway, binds to the same portion of c-Myc in vitro, In addition we were able to precipitate native c-Myc/Raf complex from various cell lysates. Physical interaction of Myc and Raf may potentially be a part of their well-known functional cooperation. (C) 1997 Federation of European Biochemical Societies.

引用

页码：465 / 470

页数：6

共 43 条

[1]

ALEXANDROVA N, 1995, MOL CELL BIOL, V15, P5188

[2] HUMAN C-MYC GENE CONTAINS A REGULATORY SITE SIMILAR TO CONSENSUS OF INTERFERON RESPONSE SEQUENCE (IRS) [J].