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    Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3

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    Authors
    Kelkar, Nyaya
    Gupta, Shashi
    Dickens, Martin
    Davis, Roger J.
    UMass Chan Affiliations
    Howard Hughes Medical Institute, Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    2000-01-11
    Keywords
    *Adaptor Proteins, Signal Transducing
    Aging
    Amino Acid Sequence
    Animals
    Brain
    Cells, Cultured
    Cloning, Molecular
    Embryonic and Fetal Development
    Enzyme Activation
    Female
    *Gene Expression Regulation, Developmental
    Gene Library
    JNK Mitogen-Activated Protein Kinases
    MAP Kinase Kinase Kinases
    Male
    Mice
    Mitogen-Activated Protein Kinases
    Molecular Sequence Data
    Nerve Tissue Proteins
    Neurons
    Protein Isoforms
    Recombinant Proteins
    Sequence Alignment
    Sequence Homology, Amino Acid
    Signal Transduction
    Life Sciences
    Medicine and Health Sciences
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    Abstract
    The c-Jun NH(2)-terminal kinase (JNK) group of mitogen-activated protein kinases (MAPKs) is activated in response to the treatment of cells with inflammatory cytokines and by exposure to environmental stress. JNK activation is mediated by a protein kinase cascade composed of a MAPK kinase and a MAPK kinase kinase. Here we describe the molecular cloning of a putative molecular scaffold protein, JIP3, that binds the protein kinase components of a JNK signaling module and facilitates JNK activation in cultured cells. JIP3 is expressed in the brain and at lower levels in the heart and other tissues. Immunofluorescence analysis demonstrated that JIP3 was present in the cytoplasm and accumulated in the growth cones of developing neurites. JIP3 is a member of a novel class of putative MAPK scaffold proteins that may regulate signal transduction by the JNK pathway.
    Source
    Mol Cell Biol. 2000 Feb;20(3):1030-43.
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/38572
    PubMed ID
    10629060
    Related Resources
    Link to Article in PubMed
    Collections
    UMass Chan Faculty and Researcher Publications

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      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.
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      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

      Molecular determinants that mediate selective activation of p38 MAP kinase isoforms

      Enslen, Herve; Brancho, Deborah Marie; Davis, Roger J. (2000-03-16)
      The p38 mitogen-activated protein kinase (MAPK) group is represented by four isoforms in mammals (p38alpha, p38beta2, p38gamma and p38delta). These p38 MAPK isoforms appear to mediate distinct functions in vivo due, in part, to differences in substrate phosphorylation by individual p38 MAPKs and also to selective activation by MAPK kinases (MAPKKs). Here we report the identification of two factors that contribute to the specificity of p38 MAPK activation. One mechanism of specificity is the selective formation of functional complexes between MAPKK and different p38 MAPKs. The formation of these complexes requires the presence of a MAPK docking site in the N-terminus of the MAPKK. The second mechanism that confers signaling specificity is the selective recognition of the activation loop (T-loop) of p38 MAPK isoforms. Together, these processes provide a mechanism that enables the selective activation of p38 MAPK in response to activated MAPKK.
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