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    Differential involvement of p38 mitogen-activated protein kinase kinases MKK3 and MKK6 in T-cell apoptosis

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    Authors
    Tanaka, Nobuyuki
    Kamanaka, Masahito
    Enslen, Herve
    Dong, Chen
    Wysk, Mark Allen
    Davis, Roger J.
    Flavell, Richard A.
    UMass Chan Affiliations
    Program in Molecular Medicine
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2002-08-02
    Keywords
    Alleles; Animals; *Apoptosis; Blotting, Western; CD4-Positive T-Lymphocytes; Calcium-Calmodulin-Dependent Protein Kinases; Cell Death; Cell Division; DNA; Down-Regulation; Enzyme Activation; Immunoblotting; Interleukin-2; Ionomycin; Ionophores; MAP Kinase Kinase 3; MAP Kinase Kinase 6; Mice; Mice, Inbred C57BL; Mice, Transgenic; Mitogen-Activated Protein Kinase Kinases; Mitogen-Activated Protein Kinases; Models, Genetic; Precipitin Tests; Protein-Tyrosine Kinases; Recombination, Genetic; T-Lymphocytes; Thymus Gland; Up-Regulation; p38 Mitogen-Activated Protein Kinases
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://dx.doi.org/10.1093/embo-reports/kvf153
    Abstract
    The p38 mitogen-activated protein kinase (p38MAPK) is activated in response to various stimuli, including cellular stress, inflammatory cytokines and cell surface receptors. The activation of p38MAPK is predominantly mediated by the two upstream MAPK kinases MKK3 and MKK6. To study the role of the p38MAPK pathway in vivo, we generated Mkk6-/- mice. We examined whether T-cell apoptosis is affected in these mice and in our previously reported Mkk3-/- mice. Strikingly, in vivo deletion of double positive thymocytes in Mkk6-/- mice was impaired, whereas Mkk3-/- mice showed no apparent abnormality. Conversely, CD4(+)T cells from Mkk3-/- but not from Mkk6-/- mice were resistant to activation-induced cell death and cytokine-withdrawal-induced apoptosis. In peripheral CD4(+)T cells, MKK3 is induced upon stimulation, whereas MKK6 is downregulated. These results suggest a novel mechanism regulating T-cell apoptosis differentially through the p38MAPK pathway by MKK3 and MKK6.
    Source
    EMBO Rep. 2002 Aug;3(8):785-91. Epub 2002 Jul 15. Link to article on publisher's site
    DOI
    10.1093/embo-reports/kvf153
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32667
    PubMed ID
    12151339
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1093/embo-reports/kvf153
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      The c-Jun NH2-terminal kinase (JNK) group of mitogen-activated protein (MAP) kinases is activated by the exposure of cells to multiple forms of stress. A putative scaffold protein was identified that interacts with multiple components of the JNK signaling pathway, including the mixed-lineage group of MAP kinase kinase kinases (MLK), the MAP kinase kinase MKK7, and the MAP kinase JNK. This scaffold protein selectively enhanced JNK activation by the MLK signaling pathway. These data establish that a mammalian scaffold protein can mediate activation of a MAP kinase signaling pathway.
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      Molecular determinants that mediate selective activation of p38 MAP kinase isoforms

      Enslen, Herve; Brancho, Deborah Marie; Davis, Roger J. (2000-03-16)
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      Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6

      Enslen, Herve; Raingeaud, Joel; Davis, Roger J. (1998-01-27)
      The cellular response to treatment with proinflammatory cytokines or exposure to environmental stress is mediated, in part, by the p38 group of mitogen-activated protein (MAP) kinases. We report the molecular cloning of a novel isoform of p38 MAP kinase, p38 beta 2. This p38 MAP kinase, like p38 alpha, is inhibited by the pyridinyl imidazole drug SB203580. The p38 MAP kinase kinase MKK6 is identified as a common activator of p38 alpha, p38 beta 2, and p38 gamma MAP kinase isoforms, while MKK3 activates only p38 alpha and p38 gamma MAP kinase isoforms. The MKK3 and MKK6 signal transduction pathways are therefore coupled to distinct, but overlapping, groups of p38 MAP kinases.
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