IDENTIFICATION OF MAPKAP KINASE-2 AS A MAJOR ENZYME RESPONSIBLE FOR THE PHOSPHORYLATION OF THE SMALL MAMMALIAN HEAT-SHOCK PROTEINS

被引：486

作者：

STOKOE, D ^{[1
]}

ENGEL, K ^{[1
]}

CAMPBELL, DG ^{[1
]}

COHEN, P ^{[1
]}

GAESTEL, M ^{[1
]}

机构：

[1] MAX DELBRUCK CTR MOLEC MED,BERLIN,GERMANY

来源：

FEBS LETTERS | 1992年 / 313卷 / 03期

基金：

英国医学研究理事会;

关键词：

MAP KINASE; PROTEIN KINASE; HEAT SHOCK; PROTEIN PHOSPHORYLATION; GROWTH FACTOR;

D O I：

10.1016/0014-5793(92)81216-9

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：

MAP kinase-activated protein kinase-2 (MAPKAP kinase-2) phosphorylates the serine residues in murine heat shock protein 25 (hsp 25) and human heat shock protein 27 (hsp27) which are phosphorylated in vivo in response to growth factors and heat shock, namely Ser15 and Ser86 (hsp25) and Ser15, Ser78 and Ser82 (hsp27). Ser86 of hsp25 and the equivalent residue in hsp27 (Ser82) are phosphorylated preferentially in vitro. The small heat shock protein is present in rabbit skeletal muscle and hsp25 kinase activity in skeletal muscle extracts co-purifies with MAPKAP kinase-2 activity throughout the purification of the latter enzyme. These results suggest that MAPKAP kinase-2 is the enzyme responsible for the phosphorylation of these small heat shock proteins in mammalian cells.

引用

页码：307 / 313

页数：7

共 30 条

[11]

GAESTEL M, 1991, J BIOL CHEM, V266, P14721

[12] MOLECULAR-CLONING, SEQUENCING AND EXPRESSION IN ESCHERICHIA-COLI OF THE 25-KDA GROWTH-RELATED PROTEIN OF EHRLICH ASCITES TUMOR AND ITS HOMOLOGY TO MAMMALIAN STRESS PROTEINS [J].