Shirin Doroudgar and Christopher C. Glembotski Stress Response Atf6 and Thrombospondin 4 : the Dynamic Duo of the Adaptive Endoplasmic Reticulum
نویسنده
چکیده
Stress Response ATF6 and Thrombospondin 4 : The Dynamic Duo of the Adaptive Endoplasmic Reticulum Print ISSN: 0009-7330. Online ISSN: 1524-4571 Copyright © 2013 American Heart Association, Inc. All rights reserved. is published by the American Heart Association, 7272 Greenville Avenue, Dallas, TX 75231 Circulation Research doi: 10.1161/CIRCRESAHA.112.28056
منابع مشابه
Ischemia 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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RATIONALE Endoplasmic reticulum (ER) stress causes the accumulation of misfolded proteins in the ER, activating the transcription factor, ATF6 (activating transcription factor 6 alpha), which induces ER stress response genes. Myocardial ischemia induces the ER stress response; however, neither the function of this response nor whether it is mediated by ATF6 is known. OBJECTIVE Here, we examin...
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Secreted and membrane proteins play critical roles in myocardial health and disease. Studies in non-myocytes have shown that the peri-nuclear ER is the site for synthesis, folding, and quality control of most secreted and membrane proteins, as well as a nexus of a signal transduction system, called the ER stress response, which informs the cell about the status of ER protein folding. Moreover, ...
متن کاملHrd1 and ER-Associated Protein Degradation, ERAD, are Critical Elements of the Adaptive ER Stress Response in Cardiac Myocytes.
RATIONALE Hydroxymethyl glutaryl-coenzyme A reductase degradation protein 1 (Hrd1) is an endoplasmic reticulum (ER)-transmembrane E3 ubiquitin ligase that has been studied in yeast, where it contributes to ER protein quality control by ER-associated degradation (ERAD) of misfolded proteins that accumulate during ER stress. Neither Hrd1 nor ERAD has been studied in the heart, or in cardiac myocy...
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...
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