{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Casey AK"],"funding":["NEI NIH HHS","NIGMS NIH HHS"],"pagination":["e2208317119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9371680"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["119(32)"],"pubmed_abstract":["The proper balance of synthesis, folding, modification, and degradation of proteins, also known as protein homeostasis, is vital to cellular health and function. The unfolded protein response (UPR) is activated when the mechanisms maintaining protein homeostasis in the endoplasmic reticulum become overwhelmed. However, prolonged or strong UPR responses can result in elevated inflammation and cellular damage. Previously, we discovered that the enzyme filamentation induced by cyclic-AMP (Fic) can modulate the UPR response via posttranslational modification of binding immunoglobulin protein (BiP) by AMPylation during homeostasis and deAMPylation during stress. Loss of <i>fic</i> in <i>Drosophila</i> leads to vision defects and altered UPR activation in the fly eye. To investigate the importan"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Fic-mediated AMPylation tempers the unfolded protein response during physiological stress."],"pmcid":["PMC9371680"],"funding_grant_id":["R01 EY010199","T32 GM127216"],"pubmed_authors":["Blevins A","Moehlman AT","Fields HA","Orth K","Gray HF","Gulen B","Casey AK","Hernandez G","Evers BM","Stewart N","Stefanius K","Servage KA","Chimalapati S","Kramer H"],"additional_accession":[]},"is_claimable":false,"name":"Fic-mediated AMPylation tempers the unfolded protein response during physiological stress.","description":"The proper balance of synthesis, folding, modification, and degradation of proteins, also known as protein homeostasis, is vital to cellular health and function. The unfolded protein response (UPR) is activated when the mechanisms maintaining protein homeostasis in the endoplasmic reticulum become overwhelmed. However, prolonged or strong UPR responses can result in elevated inflammation and cellular damage. Previously, we discovered that the enzyme filamentation induced by cyclic-AMP (Fic) can modulate the UPR response via posttranslational modification of binding immunoglobulin protein (BiP) by AMPylation during homeostasis and deAMPylation during stress. Loss of <i>fic</i> in <i>Drosophila</i> leads to vision defects and altered UPR activation in the fly eye. To investigate the importan","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2025-04-27T03:20:39.91Z","creation":"2025-04-06T18:48:05.922Z"},"accession":"S-EPMC9371680","cross_references":{"pubmed":["35914137"],"doi":["10.1073/pnas.2208317119"]}}