alexa Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.
Molecular Biology

Molecular Biology

Journal of Cell Science & Therapy

Author(s): Urano F, Wang X, Bertolotti A, Zhang Y, Chung P,

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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 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.
This article was published in Science and referenced in Journal of Cell Science & Therapy

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