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Publication : Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.

First Author  Urano F Year  2000
Journal  Science Volume  287
Issue  5453 Pages  664-6
PubMed ID  10650002 Mgi Jnum  J:132966
Mgi Id  MGI:3777353 Doi  10.1126/science.287.5453.664
Citation  Urano F, et al. (2000) Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287(5453):664-6
abstractText  Malfolded proteins in the endoplasmic reticulum (ER) induce cellular stress and activate c-Jun amino-terminal kinases (JNKs or SAPKs). Mammalian homologs of yeast IRE1, which activate chaperone genes in response to ER stress, also activated JNK, and IRE1alpha-/- fibroblasts were impaired in JNK activation by ER stress. The cytoplasmic part of IRE1 bound TRAF2, an adaptor protein that couples plasma membrane receptors to JNK activation. Dominant-negative TRAF2 inhibited activation of JNK by IRE1. Activation of JNK by endogenous signals initiated in the ER proceeds by a pathway similar to that initiated by cell surface receptors in response to extracellular signals.
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