RAP1-B IS PHOSPHORYLATED BY PROTEIN KINASE-A IN INTACT HUMAN PLATELETS

被引:72
作者
SIESS, W [1 ]
WINEGAR, DA [1 ]
LAPETINA, EG [1 ]
机构
[1] BURROUGHS WELLCOME CO,DIV CELL BIOL,RES TRIANGLE PK,NC 27709
关键词
D O I
10.1016/0006-291X(90)92182-Y
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
Agonists that increase cAMP levels in platelets promote the phosphorylation of a 24 kDa GTP-bindng protein that is immunoreactive with a monoclonal antibody (M90) to the H-ras p21 protein. Evidence is presented which indicates that this protein is rap-1b, not rap1-a as previously suggested (Ohmori, T., Kikuchi, A., Yamamoto, K., Kawata, M., Kondo, J. and Takai, Y. (1988) Biochem. Biophys. Res. Commun. 157, 670-676). The amino acid sequence of labeled peptides obtained by proteolytic cleavage of the purified phosphorylated protein was identical with that of rap-1b. Furthermore, a comparison of the kinetics of phosphorylation of synthetic peptides corresponding to the C-terminal region of rap-1a and rap-1b proteins indicated that rap-1b is the preferred substrate for phosphorylation by cAMP-dependent protein kinase. © 1990.
引用
收藏
页码:944 / 950
页数:7
相关论文
共 28 条