{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fusakio ME"],"funding":["BLRD VA","NICHD NIH HHS","NIDDK NIH HHS","RRD VA","NIAMS NIH HHS","NIGMS NIH HHS"],"pagination":["1536-51"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4850040"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["27(9)"],"pubmed_abstract":["Disturbances in protein folding and membrane compositions in the endoplasmic reticulum (ER) elicit the unfolded protein response (UPR). Each of three UPR sensory proteins-PERK (PEK/EIF2AK3), IRE1, and ATF6-is activated by ER stress. PERK phosphorylation of eIF2 represses global protein synthesis, lowering influx of nascent polypeptides into the stressed ER, coincident with preferential translation of ATF4 (CREB2). In cultured cells, ATF4 induces transcriptional expression of genes directed by the PERK arm of the UPR, including genes involved in amino acid metabolism, resistance to oxidative stress, and the proapoptotic transcription factor CHOP (GADD153/DDIT3). In this study, we characterize whole-body and tissue-specific ATF4-knockout mice and show in liver exposed to ER stress that ATF4 "],"journal":["Molecular biology of the cell"],"pubmed_title":["Transcription factor ATF4 directs basal and stress-induced gene expression in the unfolded protein response and cholesterol metabolism in the liver."],"pmcid":["PMC4850040"],"funding_grant_id":["I01 RX001477","R01 AR059115","R01 HD070487","R01 GM049164","T32 DK064466","I01 BX000976"],"pubmed_authors":["Adams CM","Mirek ET","Wek RC","Fusakio ME","Anthony TG","Willy JA","Wang Y","Al Baghdadi RJ"],"additional_accession":[]},"is_claimable":false,"name":"Transcription factor ATF4 directs basal and stress-induced gene expression in the unfolded protein response and cholesterol metabolism in the liver.","description":"Disturbances in protein folding and membrane compositions in the endoplasmic reticulum (ER) elicit the unfolded protein response (UPR). Each of three UPR sensory proteins-PERK (PEK/EIF2AK3), IRE1, and ATF6-is activated by ER stress. PERK phosphorylation of eIF2 represses global protein synthesis, lowering influx of nascent polypeptides into the stressed ER, coincident with preferential translation of ATF4 (CREB2). In cultured cells, ATF4 induces transcriptional expression of genes directed by the PERK arm of the UPR, including genes involved in amino acid metabolism, resistance to oxidative stress, and the proapoptotic transcription factor CHOP (GADD153/DDIT3). In this study, we characterize whole-body and tissue-specific ATF4-knockout mice and show in liver exposed to ER stress that ATF4 ","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 May","modification":"2026-05-30T11:23:13.715Z","creation":"2019-03-27T02:12:40Z"},"accession":"S-EPMC4850040","cross_references":{"pubmed":["26960794"],"doi":["10.1091/mbc.E16-01-0039"]}}