Activation of ATF6 and an ATF6 DNA Binding Site by the Endoplasmic Reticulum Stress Response
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منابع مشابه
The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress. Running title: The ISR facilitates activation of ATF6
The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress. Running title: The ISR facilitates activation of ATF6 Brian F. Teske, Sheree A. Wek, Piyawan Bunpo, Judy K. Cundiff, Jeanette N. McClintick, Tracy G. Anthony, and Ronald C. Wek Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianap...
متن کاملStable binding of ATF6 to BiP in the endoplasmic reticulum stress response.
Endoplasmic reticulum (ER) stress-induced activation of ATF6, an ER membrane-bound transcription factor, requires a dissociation step from its inhibitory regulator, BiP. It has been generally postulated that dissociation of the BiP-ATF6 complex is a result of the competitive binding of misfolded proteins generated during ER stress. Here we present evidence against this model and for an active r...
متن کاملEffects of the Isoform-specific Characteristics of ATF6 and ATF6 on Endoplasmic Reticulum Stress Response Gene Expression and Cell Viability*
The endoplasmic reticulum (ER)-transmembrane proteins, ATF6 and ATF6 , are cleaved during the ER stress response (ERSR). The resulting N-terminal fragments (N-ATF6 and N-ATF6 ) have conserved DNA-binding domains and divergent transcriptional activation domains. N-ATF6 and N-ATF6 translocate to the nucleus, bind to specific regulatory elements, and influence expression of ERSR genes, such as glu...
متن کاملThe eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress
Disruptions of the endoplasmic reticulum (ER) that perturb protein folding cause ER stress and elicit an unfolded protein response (UPR) that involves translational and transcriptional changes in gene expression aimed at expanding the ER processing capacity and alleviating cellular injury. Three ER stress sensors (PERK, ATF6, and IRE1) implement the UPR. PERK phosphorylation of the α subunit of...
متن کاملIschemia activates the ATF6 branch of the endoplasmic reticulum stress response.
Stresses that perturb the folding of nascent endoplasmic reticulum (ER) proteins activate the ER stress response. Upon ER stress, ER-associated ATF6 is cleaved; the resulting active cytosolic fragment of ATF6 translocates to the nucleus, binds to ER stress response elements (ERSEs), and induces genes, including the ER-targeted chaperone, GRP78. Recent studies showed that nutrient and oxygen sta...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)61473-0