Journal
SCIENCE
Volume 287, Issue 5453, Pages 664-666Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.287.5453.664
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Funding
- NIDDK NIH HHS [DK47119] Funding Source: Medline
- NIEHS NIH HHS [ES08681] Funding Source: Medline
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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 INK, and IRE1 alpha(-/-) 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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