RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase under dominant control of p38alpha mitogen-activated protein kinase (p38alphaMAPK).
A novel ribosomal S6 kinase (RSK) family member, RSK-B, was identified in a p38alphaMAPK-baited intracellular interaction screen. RSK-B presents two catalytic domains typical for the RSK family. The protein kinase C-like N-terminal and the calcium/calmodulin kinase-like C-terminal domains both contain conserved ATP-binding and activation consensus sequences. RSK-B is a p38alphaMAPK ... substrate, and activated by p38alphaMAPK and, more weakly, by ERK1. RSK-B phosphorylates the cAMP response element-binding protein (CREB) and c-Fos peptides. In intracellular assays, RSK-B drives cAMP response element- and AP1-dependent reporter expression. RSK-B locates to the cell nucleus and co-translocates p38alphaMAPK. In conclusion, RSK-B is a novel CREB kinase under dominant p38alphaMAPK control, also phosphorylating additional substrates.
Mesh Terms:
Amino Acid Sequence, Base Sequence, Calcium-Calmodulin-Dependent Protein Kinases, Cell Line, DNA Primers, Fluorescent Antibody Technique, Genes, Dominant, Humans, Mitogen-Activated Protein Kinases, Molecular Sequence Data, Recombinant Proteins, Ribosomal Protein S6 Kinases, Sequence Homology, Amino Acid, Substrate Specificity, Transcription, Genetic, p38 Mitogen-Activated Protein Kinases
Amino Acid Sequence, Base Sequence, Calcium-Calmodulin-Dependent Protein Kinases, Cell Line, DNA Primers, Fluorescent Antibody Technique, Genes, Dominant, Humans, Mitogen-Activated Protein Kinases, Molecular Sequence Data, Recombinant Proteins, Ribosomal Protein S6 Kinases, Sequence Homology, Amino Acid, Substrate Specificity, Transcription, Genetic, p38 Mitogen-Activated Protein Kinases
J. Biol. Chem.
Date: Nov. 06, 1998
PubMed ID: 9792677
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