{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Koeppen K"],"funding":["NIDDK NIH HHS","NHLBI NIH HHS","National Institutes of Health","NIGMS NIH HHS"],"pagination":["17142-50"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4059155"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["289(24)"],"pubmed_abstract":["The glucocorticoid dexamethasone increases cystic fibrosis transmembrane conductance regulator (CFTR) abundance in human airway epithelial cells by a mechanism that requires serum- and glucocorticoid-induced protein kinase 1 (SGK1) activity. The goal of this study was to determine whether SGK1 increases CFTR abundance by phosphorylating Shank2E, a PDZ domain protein that contains two SGK1 phosphorylation consensus sites. We found that SGK1 phosphorylates Shank2E as well as a peptide containing the first SGK1 consensus motif of Shank2E. The dexamethasone-induced increase in CFTR abundance was diminished by overexpression of a dominant-negative Shank2E in which the SGK1 phosphorylation sites had been mutated. siRNA-mediated reduction of Shank2E also reduced the dexamethasone-induced increase"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Serum- and glucocorticoid-induced protein kinase 1 (SGK1) increases the cystic fibrosis transmembrane conductance regulator (CFTR) in airway epithelial cells by phosphorylating Shank2E protein."],"pmcid":["PMC4059155"],"funding_grant_id":["R01-DK/HL45881","R01 DK075309","P30 GM106394","R01-HL074175","R01-DK075309","P30GM106394","R01 HL074175"],"pubmed_authors":["Stanton BA","Koeppen K","Coutermarsh BA","Madden DR"],"additional_accession":[]},"is_claimable":false,"name":"Serum- and glucocorticoid-induced protein kinase 1 (SGK1) increases the cystic fibrosis transmembrane conductance regulator (CFTR) in airway epithelial cells by phosphorylating Shank2E protein.","description":"The glucocorticoid dexamethasone increases cystic fibrosis transmembrane conductance regulator (CFTR) abundance in human airway epithelial cells by a mechanism that requires serum- and glucocorticoid-induced protein kinase 1 (SGK1) activity. The goal of this study was to determine whether SGK1 increases CFTR abundance by phosphorylating Shank2E, a PDZ domain protein that contains two SGK1 phosphorylation consensus sites. We found that SGK1 phosphorylates Shank2E as well as a peptide containing the first SGK1 consensus motif of Shank2E. The dexamethasone-induced increase in CFTR abundance was diminished by overexpression of a dominant-negative Shank2E in which the SGK1 phosphorylation sites had been mutated. siRNA-mediated reduction of Shank2E also reduced the dexamethasone-induced increase","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Jun","modification":"2025-04-18T17:58:09.743Z","creation":"2019-06-06T12:54:27Z"},"accession":"S-EPMC4059155","cross_references":{"pubmed":["24811177"],"doi":["10.1074/jbc.M114.555599","10.1074/jbc.m114.555599"]}}