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    Requirement of JNK for stress-induced activation of the cytochrome c-mediated death pathway

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    Authors
    Tournier, Cathy
    Hess, Patricia M.
    Yang, Derek D.
    Xu, Jie
    Turner, Tod K.
    Nimnual, Anjaruwee S.
    Bar-Sagi, Dafna
    Jones, Stephen N.
    Flavell, Richard A.
    Davis, Roger J.
    UMass Chan Affiliations
    Department of Cell Biology
    Department of Biochemistry and Molecular Pharmacology
    Howard Hughes Medical Institute and Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    2000-05-08
    Keywords
    Animals
    *Apoptosis
    Apoptotic Protease-Activating Factor 1
    Caspase 3
    Caspase 9
    Caspases
    Cell Count
    Cell Division
    Cells, Cultured
    Cytochrome c Group
    DNA Fragmentation
    Enzyme Activation
    Fibroblasts
    Gene Targeting
    JNK Mitogen-Activated Protein Kinases
    MAP Kinase Signaling System
    Methyl Methanesulfonate
    Mice
    Mitochondria
    Mitogen-Activated Protein Kinases
    NF-kappa B
    *Protein-Serine-Threonine Kinases
    Proteins
    Proto-Oncogene Proteins
    Proto-Oncogene Proteins c-akt
    Proto-Oncogene Proteins c-bcl-2
    Tumor Suppressor Protein p53
    Ultraviolet Rays
    Life Sciences
    Medicine and Health Sciences
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    Link to Full Text
    https://doi.org/10.1126/science.288.5467.870
    Abstract
    The c-Jun NH2-terminal kinase (JNK) is activated when cells are exposed to ultraviolet (UV) radiation. However, the functional consequence of JNK activation in UV-irradiated cells has not been established. It is shown here that JNK is required for UV-induced apoptosis in primary murine embryonic fibroblasts. Fibroblasts with simultaneous targeted disruptions of all the functional Jnk genes were protected against UV-stimulated apoptosis. The absence of JNK caused a defect in the mitochondrial death signaling pathway, including the failure to release cytochrome c. These data indicate that mitochondria are influenced by proapoptotic signal transduction through the JNK pathway.
    Source

    Science. 2000 May 5;288(5467):870-4.

    DOI
    10.1126/science.288.5467.870
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/38797
    PubMed ID
    10797012
    Related Resources

    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1126/science.288.5467.870
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      Role of p38 and JNK mitogen-activated protein kinases in the activation of ternary complex factors

      Whitmarsh, Alan J.; Yang, Shen-Hsi; Su, Michael S. S.; Sharrocks, Andrew D.; Davis, Roger J. (1997-05-01)
      The transcription factors Elk-1 and SAP-1 bind together with serum response factor to the serum response element present in the c-fos promoter and mediate increased gene expression. The ERK, JNK, and p38 groups of mitogen-activated protein (MAP) kinases phosphorylate and activate Elk-1 in response to a variety of extracellular stimuli. In contrast, SAP-1 is activated by ERK and p38 MAP kinases but not by JNK. The proinflammatory cytokine interleukin-1 (IL-1) activates JNK and p38 MAP kinases and induces the transcriptional activity of Elk-1 and SAP-1. These effects of IL-1 appear to be mediated by Rho family GTPases. To examine the relative roles of the JNK and p38 MAP kinase pathways, we examined the effects of IL-1 on CHO and NIH 3T3 cells. Studies of NIH 3T3 cells demonstrated that both the JNK and p38 MAP kinases are required for IL-1-stimulated Elk-1 transcriptional activity, while only p38 MAP kinase contributes to IL-1-induced activation of SAP-1. In contrast, studies of CHO cells demonstrated that JNK (but not the p38 MAP kinase) is required for IL-1-stimulated Elk-1-dependent gene expression and that neither JNK nor p38 MAP kinase is required for IL-1 signaling to SAP-1. We conclude that (i) distinct MAP kinase signal transduction pathways mediate IL-1 signaling to ternary complex transcription factors (TCFs) in different cell types and (ii) individual TCFs show different responses to the JNK and p38 signaling pathways. The differential utilization of TCF proteins and MAP kinase signaling pathways represents a potential mechanism for the determination of cell-type-specific responses to extracellular stimuli.
    • Thumbnail

      A cytoplasmic inhibitor of the JNK signal transduction pathway

      Dickens, Martin; Rogers, Jeffrey Scott; Cavanagh, Julie; Raitano, Art; Xia, Zhengui; Halpern, Jocelyn R.; Greenberg, Michael E.; Sawyers, Charles L.; Davis, Roger J. (1997-08-01)
      The c-Jun amino-terminal kinase (JNK) is a member of the stress-activated group of mitogen-activated protein (MAP) kinases that are implicated in the control of cell growth. A murine cytoplasmic protein that binds specifically to JNK [the JNK interacting protein-1 (JIP-1)] was characterized and cloned. JIP-1 caused cytoplasmic retention of JNK and inhibition of JNK-regulated gene expression. In addition, JIP-1 suppressed the effects of the JNK signaling pathway on cellular proliferation, including transformation by the Bcr-Abl oncogene. This analysis identifies JIP-1 as a specific inhibitor of the JNK signal transduction pathway and establishes protein targeting as a mechanism that regulates signaling by stress-activated MAP kinases.
    • Thumbnail

      Selective interaction of JNK protein kinase isoforms with transcription factors

      Gupta, Shashi; Barrett, Tamera; Whitmarsh, Alan J.; Cavanagh, Julie; Sluss, Hayla Karen; Derijard, Benoit; Davis, Roger J. (1996-06-03)
      The JNK protein kinase is a member of the MAP kinase group that is activated in response to dual phosphorylation on threonine and tyrosine. Ten JNK isoforms were identified in human brain by molecular cloning. These protein kinases correspond to alternatively spliced isoforms derived from the JNK1, JNK2 and JNK3 genes. The protein kinase activity of these JNK isoforms was measured using the transcription factors ATF2, Elk-1 and members of the Jun family as substrates. Treatment of cells with interleukin-1 (IL-1) caused activation of the JNK isoforms. This activation was blocked by expression of the MAP kinase phosphatase MKP-1. Comparison of the binding activity of the JNK isoforms demonstrated that the JNK proteins differ in their interaction with ATF2, Elk-1 and Jun transcription factors. Individual members of the JNK group may therefore selectively target specific transcription factors in vivo.
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