A cytoplasmic inhibitor of the JNK signal transduction pathway
Biochemistry & Molecular Pharmacology
Graduate School of Biomedical Sciences; Howard Hughes Medical Institute and Program in Molecular Medicine
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.
DOI of Published Version
Science. 1997 Aug 1;277(5326):693-6.
Science (New York, N.Y.)
Dickens M, Rogers JS, Cavanagh J, Raitano A, Xia Z, Halpern JR, Greenberg ME, Sawyers CL, Davis RJ. (1997). A cytoplasmic inhibitor of the JNK signal transduction pathway. GSBS Student Publications. https://doi.org/10.1126/science.277.5326.693. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/308