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
收藏
页码：10947 / 10951
页数：5
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