{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Snider NT"],"funding":["NIDDK NIH HHS"],"pagination":["241-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3563689"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["200(3)"],"pubmed_abstract":["Lysine acetylation is an important posttranslational modification that regulates microtubules and microfilaments, but its effects on intermediate filament proteins (IFs) are unknown. We investigated the regulation of keratin 8 (K8), a type II simple epithelial IF, by lysine acetylation. K8 was basally acetylated and the highly conserved Lys-207 was a major acetylation site. K8 acetylation regulated filament organization and decreased keratin solubility. Acetylation of K8 was rapidly responsive to changes in glucose levels and was up-regulated in response to nicotinamide adenine dinucleotide (NAD) depletion and in diabetic mouse and human livers. The NAD-dependent deacetylase sirtuin 2 (SIRT2) associated with and deacetylated K8. Pharmacologic or genetic inhibition of SIRT2 decreased K8 sol"],"journal":["The Journal of cell biology"],"pubmed_title":["Glucose and SIRT2 reciprocally mediate the regulation of keratin 8 by lysine acetylation."],"pmcid":["PMC3563689"],"funding_grant_id":["P30 DK34933","K01 DK093776","P30 DK034933","R01 DK52951","R01 DK052951"],"pubmed_authors":["Omary MB","Snider NT","Griggs NW","Rui L","Kwan R","Leonard JM"],"additional_accession":[]},"is_claimable":false,"name":"Glucose and SIRT2 reciprocally mediate the regulation of keratin 8 by lysine acetylation.","description":"Lysine acetylation is an important posttranslational modification that regulates microtubules and microfilaments, but its effects on intermediate filament proteins (IFs) are unknown. We investigated the regulation of keratin 8 (K8), a type II simple epithelial IF, by lysine acetylation. K8 was basally acetylated and the highly conserved Lys-207 was a major acetylation site. K8 acetylation regulated filament organization and decreased keratin solubility. Acetylation of K8 was rapidly responsive to changes in glucose levels and was up-regulated in response to nicotinamide adenine dinucleotide (NAD) depletion and in diabetic mouse and human livers. The NAD-dependent deacetylase sirtuin 2 (SIRT2) associated with and deacetylated K8. Pharmacologic or genetic inhibition of SIRT2 decreased K8 sol","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Feb","modification":"2025-05-18T11:57:45.896Z","creation":"2025-05-18T11:57:45.896Z"},"accession":"S-EPMC3563689","cross_references":{"pubmed":["23358244"],"doi":["10.1083/jcb.201209028"]}}