A cytoplasmic inhibitor of the JNK signal transduction pathway Academic Article Article uri icon

Overview

MeSH Major

  • Apoptosis
  • Apoptosis Regulatory Proteins
  • Carcinoma, Non-Small-Cell Lung
  • Drug Resistance, Neoplasm
  • Leukemia, Myelogenous, Chronic, BCR-ABL Positive
  • Lung Neoplasms
  • Membrane Proteins
  • Polymorphism, Genetic
  • Protein Kinase Inhibitors
  • Proto-Oncogene Proteins
  • Sequence Deletion

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 date

  • August 1997

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1126/science.277.5326.693

PubMed ID

  • 9235893

Additional Document Info

start page

  • 693

end page

  • 6

volume

  • 277

number

  • 5326