Stable Binding of ATF6 to BiP in the Endoplasmic Reticulum Stress Response
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چکیده
منابع مشابه
Stable 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...
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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...
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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...
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ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 2005
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.25.3.921-932.2005