{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gulen B"],"funding":["Welch Foundation (The Welch Foundation)","NIH GM","Once Upon A Time Foundation","Welch Foundation","NIGMS NIH HHS"],"pagination":["e2400781121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11420183"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(38)"],"pubmed_abstract":["During homeostasis, the endoplasmic reticulum (ER) maintains productive transmembrane and secretory protein folding that is vital for proper cellular function. The ER-resident HSP70 chaperone, binding immunoglobulin protein (BiP), plays a pivotal role in sensing ER stress to activate the unfolded protein response (UPR). BiP function is regulated by the bifunctional enzyme filamentation induced by cyclic-AMP domain protein (FicD) that mediates AMPylation and deAMPylation of BiP in response to changes in ER stress. AMPylated BiP acts as a molecular rheostat to regulate UPR signaling, yet little is known about the molecular consequences of FicD loss. In this study, we investigate the role of FicD in mouse embryonic fibroblast (MEF) response to pharmacologically and metabolically induced ER st"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["FicD sensitizes cellular response to glucose fluctuations in mouse embryonic fibroblasts."],"pmcid":["PMC11420183"],"funding_grant_id":["I-1561","NA","R35 GM134945","T32 GM127216"],"pubmed_authors":["Kinch LN","Blevins A","Servage KA","Orth K","Gray HF","Gulen B","Casey AK","Stewart NM"],"additional_accession":[]},"is_claimable":false,"name":"FicD sensitizes cellular response to glucose fluctuations in mouse embryonic fibroblasts.","description":"During homeostasis, the endoplasmic reticulum (ER) maintains productive transmembrane and secretory protein folding that is vital for proper cellular function. The ER-resident HSP70 chaperone, binding immunoglobulin protein (BiP), plays a pivotal role in sensing ER stress to activate the unfolded protein response (UPR). BiP function is regulated by the bifunctional enzyme filamentation induced by cyclic-AMP domain protein (FicD) that mediates AMPylation and deAMPylation of BiP in response to changes in ER stress. AMPylated BiP acts as a molecular rheostat to regulate UPR signaling, yet little is known about the molecular consequences of FicD loss. In this study, we investigate the role of FicD in mouse embryonic fibroblast (MEF) response to pharmacologically and metabolically induced ER st","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Sep","modification":"2025-04-19T19:29:54.842Z","creation":"2025-04-19T19:29:54.842Z"},"accession":"S-EPMC11420183","cross_references":{"pubmed":["39259589"],"doi":["10.1073/pnas.2400781121"]}}