GSBS Student Publications


A cytoplasmic inhibitor of the JNK signal transduction pathway

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Graduate School of Biomedical Sciences; Howard Hughes Medical Institute and Program in Molecular Medicine



Document Type


Medical Subject Headings

Activating Transcription Factor 2; Animals; COS Cells; Calcium-Calmodulin-Dependent Protein Kinases; Carrier Proteins; Cell Nucleus; Cell Transformation, Neoplastic; Cells, Cultured; Cloning, Molecular; Cyclic AMP Response Element-Binding Protein; Cytoplasm; Fusion Proteins, bcr-abl; Gene Expression Regulation; JNK Mitogen-Activated Protein Kinases; Mitogen-Activated Protein Kinase 9; *Mitogen-Activated Protein Kinases; Molecular Sequence Data; Phosphorylation; Protein Kinases; Proto-Oncogene Proteins c-jun; Recombinant Fusion Proteins; *Signal Transduction; Trans-Activation (Genetics); Transcription Factors; Transfection


Life Sciences | Medicine and Health Sciences


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.

Rights and Permissions

Citation: Science. 1997 Aug 1;277(5326):693-6.

Related Resources

Link to article in PubMed

Journal Title

Science (New York, N.Y.)

PubMed ID