Basic Fibroblast Growth Factor-induced Activation of Novel CREB Kinase during the Differentiation of Immortalized Hippocampal Cells

Autor: Song Woo Shin, Kwang Chul Chung, Jee Young Sung, Young Soo Ahn
Rok vydání: 2001
Předmět:
Time Factors
Transcription
Genetic
Mitogen-activated protein kinase kinase
Hippocampus
p38 Mitogen-Activated Protein Kinases
Biochemistry
MAP2K7
Serine
Enzyme Inhibitors
Phosphorylation
Casein Kinase II
Luciferases
Protein Kinase C
Genes
Dominant
Glutathione Transferase
biology
Chemistry
Stem Cells
Nuclear Proteins
Cell Differentiation
CREB-Binding Protein
Recombinant Proteins
Electrophoresis
Polyacrylamide Gel
Fibroblast Growth Factor 2
Mitogen-Activated Protein Kinases
Protein Binding
Signal Transduction
Blotting
Western
Protein Serine-Threonine Kinases
Transfection
CREB
Calmodulin
CREB in cognition
Animals
Molecular Biology
MAPK14
MAP kinase kinase kinase
Akt/PKB signaling pathway
Ribosomal Protein S6 Kinases
Cyclin-dependent kinase 2
Cell Biology
Cyclic AMP-Dependent Protein Kinases
Molecular biology
Rats
Enzyme Activation
Kinetics
Calcium-Calmodulin-Dependent Protein Kinases
Mutation
Trans-Activators
biology.protein
Zdroj: Journal of Biological Chemistry. 276:13858-13866
ISSN: 0021-9258
DOI: 10.1074/jbc.m010610200
Popis: Growth factors bind to their specific receptors on the responsive cell surface and thereby initiate dramatic changes in the proliferation, differentiation, and survival of their target cells. In the present study we have examined the mechanism by which growth factor-induced signals are propagated to the nucleus, leading to the activation of transcription factor, cis-acting cAMP response element (CRE)-binding protein (CREB), in immortalized hippocampal progenitor cells (H19-7). During the differentiation of H19-7 cells by basic fibroblast growth factor (bFGF) a critical regulatory Ser(133) residue of CREB was phosphorylated followed by an increase of CRE-mediated gene transcription. Expression of S133A CREB mutants blocked the differentiation of H19-7 cells by bFGF. Although the kinetics of CREB phosphorylation by EGF was transient, bFGF induced a prolonged pattern of CREB phosphorylation. Interestingly, bFGF-induced CREB phosphorylation and subsequent CRE-mediated gene transcription is not likely to be mediated by any of previously known signaling pathways that lead to phosphorylation of CREB, such as mitogen-activated protein kinases, protein kinase A, protein kinase C, phosphatidylinositol 3-kinase-p70(S6K), calcium/calmodulin dependent protein kinase, and casein kinase 2. By using in vitro in gel kinase assay the presence of a novel 120-kDa bFGF-inducible CREB kinase was identified. These findings identify a new growth factor-activated signaling pathway that regulates gene expression at the CRE.
Databáze: OpenAIRE
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