RAF-1 FORMS A STABLE COMPLEX WITH MEK1 AND ACTIVATES MEK1 BY SERINE PHOSPHORYLATION

被引：119

作者：

HUANG, WD

ALESSANDRINI, A

CREWS, CM

ERIKSON, RL

机构：

[1] Dept. of Cell. and Devmtl. Biology, Harvard University, Cambridge, MA 02138

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 23期

关键词：

MITOGEN-ACTIVATED PROTEIN KINASE; PROTEIN KINASES; SIGNAL TRANSDUCTION;

D O I：

10.1073/pnas.90.23.10947

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Recombinant Mek1 and Raf-1 proteins produced in Sf9 cells undergo a tight association both in vivo and in vitro, which apparently does not depend on additional factors or the kinase activity of Mek1 or Raf-1. The complex can be disrupted by two polyclonal antibodies raised against Raf-1 peptides. Coinfection with Raf-1 activates Mek1 >150-fold, and coinfection with Raf-1 and Mek1 activates Erk1 almost-equal-to 90-fold. The activation of Mek1 by Raf-1 involves only serine phosphorylation, which is directly proportional to the extent of Mek1 activation. Phosphopeptide maps suggest a single Raf-1 phosphorylation site on Mek1.

引用

页码：10947 / 10951

页数：5

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