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.
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| rdf:type | |
| rdfs:comment |
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.
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| skos:exactMatch | |
| uniprot:name |
Science
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| uniprot:author |
Cavanagh J.,
Davis R.J.,
Dickens M.,
Greenberg M.E.,
Halpern J.R.,
Raitano A.,
Rogers J.S.,
Sawyers C.L.,
Xia Z.
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| uniprot:date |
1997
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| uniprot:pages |
693-696
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| uniprot:title |
A cytoplasmic inhibitor of the JNK signal transduction pathway.
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| uniprot:volume |
277
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| dc-term:identifier |
doi:10.1126/science.277.5326.693
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