ROLE OF P34(CDC2)-MEDIATED PHOSPHORYLATIONS IN 2-STEP ACTIVATION OF PP60(C-SRC) DURING MITOSIS

被引：73

作者：

SHENOY, S

CHACKALAPARAMPIL, I

BAGRODIA, S

LIN, PH

SHALLOWAY, D

机构：

[1] CORNELL UNIV, BIOCHEM SECT, MOLEC & CELL BIOL LAB, ITHACA, NY 14853 USA

[2] CORNELL UNIV, DEPT PATHOL, CANC BIOL LAB, ITHACA, NY 14853 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1992年 / 89卷 / 15期

关键词：

CELL CYCLE; ONCOPROTEIN; PHOSPHOTYROSINE; TRANSFORMATION;

D O I：

10.1073/pnas.89.15.7237

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：

Phosphorylation of pp60c-src by p34cdc2 at three amino-proximal serine/threonine residues is temporally correlated with, but insufficient for, mitotic activation of c-Src kinase. The direct cause of activation during mitosis appears to be temporally correlated partial dephosphorylation of Tyr-527, a residue whose phosphorylation strongly suppresses pp60c-src activity. Site-directed mutagenesis of the serine/threonine phosphorylation sites blocks half the mitosis-specific decrease in Tyr-527 phosphorylation and half the increase in pp60c-src kinase activity. We conclude that p34cdc2 partially activates pp60c-src by a two-step process in which its serine/threonine phosphorylations either sensitize pp60c-src to a Tyr-527 phosphatase or desensitize it to a Tyr-527 kinase. Furthermore, additional events, independent of these p34cdc2-mediated phosphorylations, participate in mitotic activation of pp60c-src.

引用

页码：7237 / 7241

页数：5

共 31 条

[1] ALTERED TYROSINE-527 PHOSPHORYLATION AND MITOTIC ACTIVATION OF P60C-SRC [J].