MOUSE ERK-1 GENE-PRODUCT IS A SERINE THREONINE PROTEIN-KINASE THAT HAS THE POTENTIAL TO PHOSPHORYLATE TYROSINE

被引：118
作者：
CREWS, CM
ALESSANDRINI, AA
ERIKSON, RL
机构：
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 19期
关键词：
MAP KINASE; AUTOPHOSPHORYLATION; RIBOSOMAL PROTEIN S6 KINASE; SIGNAL TRANSDUCTION;
D O I：
10.1073/pnas.88.19.8845
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：
Bacterial expression of mouse gene Erk-1 yielded an active kinase with the same substrate specificity shown for ERK1 protein purified from rat cells. Although rat gene ERK1 is believed to encode a serine/threonine kinase based on sequence data and known ERK1 substrate phosphorylation sites, bacterially-produced mouse Erk-1 (bt-Erk-1) autophosphorylated on tyrosine in addition to serine and threonine residues. The bt-Erk-1 protein also had the capacity to reactivate the ribosomal protein S6 kinase (S6KII). Furthermore, treatment of bt-Erk-1 with either serine/threonine-specific phosphatase 2A or tyrosine-specific phosphatase 1B significantly decreased its kinase activity. These findings predict that autophosphorylation may play an important role in Erk-1/ERK1 regulation.
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页码：8845 / 8849
页数：5
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