REQUIREMENTS FOR PHOSPHORYLATION OF MAP KINASE DURING MEIOSIS IN XENOPUS OOCYTES

被引：286

作者：

POSADA, J ^{[1
]}

COOPER, JA ^{[1
]}

机构：

[1] FRED HUTCHINSON CANC RES CTR,SEATTLE,WA 98104

来源：

SCIENCE | 1992年 / 255卷 / 5041期

关键词：

D O I：

10.1126/science.1313186

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：

Mitogen-activated protein (MAP) kinases are activated in response to a variety of extracellular stimuli by phosphorylation on tyrosine and threonine residues. Xp42 is a Xenopus laevis MAP kinase that is activated during oocyte maturation. Modified forms of Xp42 that lacked enzymatic activity or either of the phosphorylation sites were expressed in Xenopus oocytes. When meiotic maturation was induced with progesterone, each mutant Xp42 was phosphorylated, indicating that at least one kinase was activated that can phosphorylate Xp42 on tyrosine and threonine. Phosphorylation of one residue is not strictly dependent on phosphorylation of the other.

引用

页码：212 / 215

页数：4

共 45 条

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