STRUCTURAL AND FUNCTIONAL-ANALYSIS OF PP70(S6K)

被引：109

作者：

CHEATHAM, L ^{[1
]}

MONFAR, M ^{[1
]}

CHOU, MM ^{[1
]}

BLENIS, J ^{[1
]}

机构：

[1] HARVARD UNIV,SCH MED,DEPT CELL BIOL,BOSTON,MA 02130

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 25期

关键词：

D O I：

10.1073/pnas.92.25.11696

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：

The pp70/85-kDa S6 kinases, collectively referred to as pp70(S6k) are thought to participate in transit through the G(1) phase of the cell cycle. pp70(S6k) regulates the phosphorylation of the 40S ribosomal protein S6 and the transcription factor CREM tau. pp70(S6k) is regulated by serine/threonine phosphorylation, and although 1-phosphatidylinositol 3-kinase and phospholipase C have been implicated as upstream regulators, the mechanism of activation and identity of the upstream pp70(S6k) kinases remain unknown. To improve our understanding of how this mitogen-stimulated protein kinase is regulated by growth factors and the immunosuppressant rapamycin, we have initiated a structure/function analysis of pp70(S6k). Our results indicate that both the N and C termini participate in the complex regulation of pp70(S6k) activity.

引用

页码：11696 / 11700

页数：5

共 30 条

[1]

BALLOU LM, 1988, J BIOL CHEM, V263, P1188

[2] MOLECULAR-STRUCTURE OF A MAJOR INSULIN MITOGEN-ACTIVATED 70-KDA S6 PROTEIN-KINASE [J].