A comparison of the substrate specificity of MAPKAP kinase‐2 and MAPKAP kinase‐3 and their activation by cytokines and cellular stress

FEBS Letters

Clifton, Andrew D.¹  Cohen, Philip¹  Young, Peter R.² 

[1] MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee, DD1 4HN Scotland, UK;SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406, USA

关键词: MAPKAP kinase;    MAP kinase;    Stress;    Cytokine;    HSP27;   

DOI  :  10.1016/0014-5793(96)00816-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

MAPKAP kinase-2 and MAPKAP kinase-3 were both activated in response to cellular stress, interleukin-1 and tumour necrosis factor in KB and HeLa cells, and with identical kinetics. Activation of MAPKAP kinase-3, like MAPKAP kinase-2, was prevented by SB 203580, a specific inhibitor of SAPK-2, the upstream activator of MAPKAP kinase-2. MAPKAP kinase-3 and MAPKAP kinase-2 phosphorylated peptide substrates with similar kinetic constants and phosphorylated the same serine residues in HSP27 at the same relative rates. These results establish that MAPKAP kinase-3 lies ‘downstream’ of SAPK-2 and that it is likely to have overlapping or identical substrates to MAPKAP kinase-2 in vivo.

【 授权许可】

Unknown