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    c-Jun N-terminal kinase (JNK) repression during the inflammatory response? Just say NO

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    Authors
    Hall, J. Perry
    Merithew, Eric Lee
    Davis, Roger J.
    UMass Chan Affiliations
    Howard Hughes Medical Institute and Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    2000-12-20
    Keywords
    Amino Acid Sequence
    Animals
    Enzyme Activation
    Interferon Type II
    JNK Mitogen-Activated Protein Kinases
    Mitogen-Activated Protein Kinase 10
    Mitogen-Activated Protein
    Kinases
    Molecular Sequence Data
    Nitric Oxide
    Nitric Oxide Donors
    Penicillamine
    Protein-Tyrosine Kinases
    Signal Transduction
    Life Sciences
    Medicine and Health Sciences
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    Link to Full Text
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC34087/
    Source

    Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14022-4. Link to article on publisher's site

    DOI
    10.1073/pnas.97.26.14022
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/38956
    PubMed ID
    11121010
    Related Resources

    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1073/pnas.97.26.14022
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    Showing items related by title, author, creator and subject.

    • Thumbnail

      Role of the JIP4 scaffold protein in the regulation of mitogen-activated protein kinase signaling pathways

      Kelkar, Nyaya; Standen, Claire L.; Davis, Roger J. (2005-03-16)
      The c-Jun NH2-terminal kinase (JNK)-interacting protein (JIP) group of scaffold proteins (JIP1, JIP2, and JIP3) can interact with components of the JNK signaling pathway and potently activate JNK. Here we describe the identification of a fourth member of the JIP family. The primary sequence of JIP4 is most closely related to that of JIP3. Like other members of the JIP family of scaffold proteins, JIP4 binds JNK and also the light chain of the microtubule motor protein kinesin-1. However, the function of JIP4 appears to be markedly different from other JIP proteins. Specifically, JIP4 does not activate JNK signaling. In contrast, JIP4 serves as an activator of the p38 mitogen-activated protein (MAP) kinase pathway by a mechanism that requires the MAP kinase kinases MKK3 and MKK6. The JIP4 scaffold protein therefore appears to be a new component of the p38 MAP kinase signaling pathway.
    • Thumbnail

      A mammalian scaffold complex that selectively mediates MAP kinase activation

      Whitmarsh, Alan J.; Cavanagh, Julie; Tournier, Cathy; Yasuda, Jun; Davis, Roger J. (1998-09-11)
      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.
    • Thumbnail

      The MKK7 gene encodes a group of c-Jun NH2-terminal kinase kinases

      Tournier, Cathy; Whitmarsh, Alan J.; Cavanagh, Julie; Barrett, Tamera; Davis, Roger J. (1999-01-16)
      The c-Jun NH2-terminal protein kinase (JNK) is a member of the mitogen-activated protein kinase (MAPK) group and is an essential component of a signaling cascade that is activated by exposure of cells to environmental stress. JNK activation is regulated by phosphorylation on both Thr and Tyr residues by a dual-specificity MAPK kinase (MAPKK). Two MAPKKs, MKK4 and MKK7, have been identified as JNK activators. Genetic studies demonstrate that MKK4 and MKK7 serve nonredundant functions as activators of JNK in vivo. We report here the molecular cloning of the gene that encodes MKK7 and demonstrate that six isoforms are created by alternative splicing to generate a group of protein kinases with three different NH2 termini (alpha, beta, and gamma isoforms) and two different COOH termini (1 and 2 isoforms). The MKK7alpha isoforms lack an NH2-terminal extension that is present in the other MKK7 isoforms. This NH2-terminal extension binds directly to the MKK7 substrate JNK. Comparison of the activities of the MKK7 isoforms demonstrates that the MKK7alpha isoforms exhibit lower activity, but a higher level of inducible fold activation, than the corresponding MKK7beta and MKK7gamma isoforms. Immunofluorescence analysis demonstrates that these MKK7 isoforms are detected in both cytoplasmic and nuclear compartments of cultured cells. The presence of MKK7 in the nucleus was not, however, required for JNK activation in vivo. These data establish that the MKK4 and MKK7 genes encode a group of protein kinases with different biochemical properties that mediate activation of JNK in response to extracellular stimuli.
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