Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Activating Transcription Factor 2
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Animals
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COS Cells
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism*
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Cell Nucleus / metabolism
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Cell Transformation, Neoplastic
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Cells, Cultured
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Cloning, Molecular
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Cyclic AMP Response Element-Binding Protein / metabolism
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Cytoplasm / metabolism
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Fusion Proteins, bcr-abl / metabolism
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Gene Expression Regulation
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JNK Mitogen-Activated Protein Kinases
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Mitogen-Activated Protein Kinase 9
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Mitogen-Activated Protein Kinases*
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Molecular Sequence Data
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Phosphorylation
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Protein Kinases / metabolism
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Proto-Oncogene Proteins c-jun / metabolism
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Recombinant Fusion Proteins / metabolism
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Signal Transduction*
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Transcription Factors / metabolism
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Transcriptional Activation
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Transfection
Substances
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Activating Transcription Factor 2
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Carrier Proteins
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Cyclic AMP Response Element-Binding Protein
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Proto-Oncogene Proteins c-jun
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Recombinant Fusion Proteins
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Transcription Factors
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Protein Kinases
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Mitogen-Activated Protein Kinase 9
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Fusion Proteins, bcr-abl
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Calcium-Calmodulin-Dependent Protein Kinases
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JNK Mitogen-Activated Protein Kinases
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Mitogen-Activated Protein Kinases