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PRAK, a novel protein kinase regulated by the p38 MAP kinase
Author(s) -
New Liguo,
Jiang Yong,
Zhao Ming,
Liu Kang,
Zhu Wei,
Flood Laura J.,
Kato Yutaka,
Parry Graham C.N.,
Han Jiahuai
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.12.3372
Subject(s) - biology , ask1 , map2k7 , protein kinase a , map kinase kinase kinase , mitogen activated protein kinase kinase , cyclin dependent kinase 2 , p38 mitogen activated protein kinases , cyclin dependent kinase 9 , kinase , autophagy related protein 13 , protein phosphorylation , mapk14 , c raf , microbiology and biotechnology , biochemistry
We have identified and cloned a novel serine/ threonine kinase, p38‐regulated/activated protein kinase (PRAK). PRAK is a 471 amino acid protein with 20–30% sequence identity to the known MAP kinase‐regulated protein kinases RSK1/2/3, MNK1/2 and MAPKAP‐K2/3. PRAK was found to be expressed in all human tissues and cell lines examined. In HeLa cells, PRAK was activated in response to cellular stress and proinflammatory cytokines. PRAK activity was regulated by p38α and p38β both in vitro and in vivo and Thr182 was shown to be the regulatory phosphorylation site. Activated PRAK in turn phosphorylated small heat shock protein 27 (HSP27) at the physiologically relevant sites. An in‐gel kinase assay demonstrated that PRAK is a major stress‐activated kinase that can phosphorylate small heat shock protein, suggesting a potential role for PRAK in mediating stress‐induced HSP27 phosphorylation in vivo .