The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase

Autor: Sally Rose, Louis C. Mahadevan, Stuart Thomson, Catherine A. Hazzalin, Alison L. Clayton, Michael J. Barratt
Rok vydání: 1999
Předmět:
Transcriptional Activation
Time Factors
Proto-Oncogene Proteins c-jun
Blotting
Western
Biology
Mitogen-activated protein kinase kinase
Models
Biological
Ribosomal Protein S6 Kinases
90-kDa
Gene Expression Regulation
Enzymologic
General Biochemistry
Genetics and Molecular Biology
MAP2K7
Histones
Mice
chemistry.chemical_compound
Animals
Enzyme Inhibitors
Phosphorylation
Genes
Immediate-Early
Molecular Biology
Cells
Cultured
Anisomycin
MAPK14
Protein Synthesis Inhibitors
Mice
Inbred C3H
Sulfonamides
General Immunology and Microbiology
MAP kinase kinase kinase
General Neuroscience
Cyclin-dependent kinase 2
High Mobility Group Proteins
Fibroblasts
Isoquinolines
Molecular biology
Nucleosomes
chemistry
Calcium-Calmodulin-Dependent Protein Kinases
biology.protein
Tetradecanoylphorbol Acetate
Cyclin-dependent kinase 9
Mitogen-Activated Protein Kinases
Proto-Oncogene Proteins c-fos
Immediate early gene
Signal Transduction
Research Article
Zdroj: The EMBO Journal. 18:4779-4793
ISSN: 1460-2075
DOI: 10.1093/emboj/18.17.4779
Popis: The nucleosomal response refers to the rapid phosphorylation of histone H3 on serine 10 and HMG-14 on serine 6 that occurs concomitantly with immediate-early (IE) gene induction in response to a wide variety of stimuli. Using antibodies against the phosphorylated residues, we show that H3 and HMG-14 phosphorylation is mediated via different MAP kinase (MAPK) cascades, depending on the stimulus. The nucleosomal response elicited by TPA is ERK-dependent, whereas that elicited by anisomycin is p38 MAPK-dependent. In intact cells, the nucleosomal response can be selectively inhibited using the protein kinase inhibitor H89. MAPK activation and phosphorylation of transcription factors are largely unaffected by H89, whereas induction of IE genes is inhibited and its characteristics markedly altered. MSK1 is considered the most likely kinase to mediate this response because (i) it is activated by both ERK and p38 MAPKs; (ii) it is an extremely efficient kinase for HMG-14 and H3, utilizing the physiologically relevant sites; and (iii) its activity towards H3/HMG-14 is uniquely sensitive to H89 inhibition. Thus, the nucleosomal response is an invariable consequence of ERK and p38 but not JNK/SAPK activation, and MSK1 potentially provides a link to complete the circuit between cell surface and nucleosome.
Databáze: OpenAIRE
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