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

Fumihiko Urano, XiaoZhong Wang, Anne Bertolotti, Yuhong Zhang, Peter Chung, Heather P. Harding, David Ron*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2099 Scopus citations

Abstract

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 IRE1α (-/-) 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.

Original languageEnglish (US)
Pages (from-to)664-666
Number of pages3
JournalScience
Volume287
Issue number5453
DOIs
StatePublished - Jan 28 2000

ASJC Scopus subject areas

  • General

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