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This occurs under physiological situations that cause an abrupt increase in protein synthesis, or under redox and metabolic stresses. Among the latter, hyperglycemia and glucose scarcity have been identified as major modulators of UPR signaling. Indeed, the first mammalian UPR effector, the glucose\u2010regulated protein 78, also known as BiP, was identified in response to glucose deprivation. Tunicamycin, arguably the most commonly used drug to induce ER stress responses\n                    <jats:italic>in vitro<\/jats:italic>\n                    and\n                    <jats:italic>in vivo<\/jats:italic>\n                    , is an inhibitor of\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation. We compile here evidence that the UPR is activated upon physiological and pathological conditions that alter glucose levels and that this is mostly mediated by alterations of protein\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation, ATP levels, or redox balance. The three branches of the UPR transduced by PERK\/ATF4, IRE1\/XBP1s, and ATF6, as well as non\u2010canonical ER sensors such as SCAP\/SREBP, sense ER protein glycosylation status driven by glucose and other glucose\u2010derived metabolites. The outcomes of UPR activation range from restoring protein\n                    <jats:italic>N<\/jats:italic>\n                    \u2010glycosylation and protein folding flux to stimulating autophagy, organelle recycling, and mitochondrial respiration, and in some cases, cell death. Anabolic responses to glucose levels are also stimulated by glucose through components of the UPR. Therefore, the UPR should be further studied as a potential biomarker and mediator of glucose\u2010associated diseases.\n                  <\/jats:p>","DOI":"10.1111\/febs.70113","type":"journal-article","created":{"date-parts":[[2025,4,24]],"date-time":"2025-04-24T08:24:53Z","timestamp":1745483093000},"page":"3581-3595","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["Glucose sensing and the unfolded protein response"],"prefix":"10.1111","volume":"292","author":[{"given":"Mabel","family":"Cruz\u2010Rodr\u00edguez","sequence":"first","affiliation":[{"name":"Preclinical and Experimental Research in Thoracic Tumors (PRETT) Group IDIBELL  L'Hospitalet de Llobregat Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5855-4522","authenticated-orcid":false,"given":"Eric","family":"Chevet","sequence":"additional","affiliation":[{"name":"INSERM U1242, Univ Rennes, Centre de 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