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regulated IRE-1 Dependent mRNA Decay

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https://www.readbyqxmd.com/read/26487694/pdia6-regulates-insulin-secretion-by-selectively-inhibiting-the-ridd-activity-of-ire1
#1
Daniela Eletto, Davide Eletto, Sarah Boyle, Yair Argon
Protein disulfide isomerase A6 (PDIA6) interacts with protein kinase RNA-like endoplasmic reticulum kinase (PERK) and inositol requiring enzyme (IRE)-1 and inhibits their unfolded protein response signaling. In this study, shRNA silencing of PDIA6 expression in insulin-producing mouse cells reduced insulin production (5-fold) and, consequently, glucose-stimulated insulin secretion (3-4-fold). This inhibition of insulin release was independent of the PDIA6-PERK interaction or PERK activity. Acute inhibition of PERK did not change the short-term response of β cells to glucose...
February 2016: FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology
https://www.readbyqxmd.com/read/25077793/mrna-decay-factor-auf1-binds-the-internal-ribosomal-entry-site-of-enterovirus-71-and-inhibits-virus-replication
#2
Jing-Yi Lin, Mei-Ling Li, Gary Brewer
AU-rich element binding factor 1 (AUF1) has a role in the replication cycles of different viruses. Here we demonstrate that AUF1 binds the internal ribosome entry site (IRES) of enterovirus 71 (EV71) and negatively regulates IRES-dependent translation. During EV71 infection, AUF1 accumulates in the cytoplasm where viral replication occurs, whereas AUF1 localizes predominantly in the nucleus in mock-infected cells. AUF1 knockdown in infected cells increases IRES activity and synthesis of viral proteins. Taken together, the results suggest that AUF1 interacts with the EV71 IRES to negatively regulate viral translation and replication...
2014: PloS One
https://www.readbyqxmd.com/read/12941295/transcriptional-and-translational-control-of-mcl-1-during-apoptosis
#3
COMPARATIVE STUDY
Daniel Iglesias-Serret, Maria Piqué, Joan Gil, Gabriel Pons, José M López
Mcl-1 is an antiapoptotic member of the Bcl-2 family whose protein and mRNA have a short half-life. In this report, we studied the changes in Mcl-1 protein and mRNA expression induced by staurosporine and aspirin. Both drugs induced apoptosis in Jurkat cells and reduced the levels of Mcl-1 protein. The caspase inhibitor Z-VAD.fmk and the proteasome inhibitor MG132 partially protected Mcl-1 from decay, indicating that both caspase-dependent and proteasome pathways are involved during apoptosis. Staurosporine also reduced Mcl-1 mRNA levels and this reduction was mostly caspase-dependent...
September 15, 2003: Archives of Biochemistry and Biophysics
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