A regulatory mechanism for RSK2 NH(2)-terminal kinase activity.

ABSTRACT: Our previous findings indicated that RSK2 plays a critical role in proliferation and cell transformation induced by tumor promoters, such as epidermal growth factor or 12-O-tetradecanoylphorbol-13-acetate, and that kaempferol, a natural compound found in edible plants, selectively inhibits RSK2 activity. However, the molecular mechanism for RSK2 activation is unclear. Herein, we provide evidence showing that NH(2)-terminal kinase domain (NTD) activation of RSK2 is required for the activation of the extracellular signal-regulated kinase-mediated COOH-terminal kinase domain (CTD). We also found that the NTD plays a key role in substrate phosphorylation and that kaempferol binds with the NTD but not the CTD in both the active and inactive forms. Homology modeling of the RSK2 NH(2)-terminal do

SUBMITTER: Cho YY 

PROVIDER: S-EPMC2822654 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature