THE PRIMARY STRUCTURE OF A HUMAN MAP KINASE ACTIVATED PROTEIN-KINASE-2

被引：49

作者：

ZU, YL ^{[1
]}

WU, FY ^{[1
]}

GILCHRIST, A ^{[1
]}

AI, YX ^{[1
]}

LABADIA, ME ^{[1
]}

HUANG, CK ^{[1
]}

机构：

[1] UNIV CONNECTICUT,CTR HLTH,DEPT PATHOL,FARMINGTON,CT 06030

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 200卷 / 02期

关键词：

D O I：

10.1006/bbrc.1994.1566

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：

Mitogen-activated protein (MAP) kinase is of central importance in mediating response to a variety of extracellular stimuli. MAP kinase activated protein (MAPKAP) kinase 2 is one of the two known protein kinases that can be phosphorylated and activated by MAP kinase. Here we present the first complete primary structure of MAPKAP kinase 2 elucidated from a human cDNA sequence. Sequence analysis reveals that MAPKAP kinase 2 is a 370 amino acid protein containing a proline-rich N-terminal region and a well conserved catalytic domain. Northern blot analysis of MAPKAP kinase 2 showed a 4.8 kb mRNA species in HL-60 cells. In addition, we also show the first evidence that recombinant MAPKAP kinase 2 is phosphorylated and activated by MAP kinase in vitro. (C) 1994 Academic Press, Inc.

引用

页码：1118 / 1124

页数：7

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