{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["24(6)"],"submitter":["Sabio G"],"pubmed_abstract":["Activation of the p38 MAP kinase pathways is crucial for the adaptation of mammalian cells to changes in the osmolarity of the environment. Here we identify SAP97/hDlg, the mammalian homologue of the Drosophila tumour suppressor Dlg, as a physiological substrate for the p38gamma MAP kinase (SAPK3/p38gamma) isoform. SAP97/hDlg is a scaffold protein that forms multiprotein complexes with a variety of proteins and is targeted to the cytoskeleton by its association with the protein guanylate kinase-associated protein (GKAP). The SAPK3/p38gamma-catalysed phosphorylation of SAP97/hDlg triggers its dissociation from GKAP and therefore releases it from the cytoskeleton. This is likely to regulate the integrity of intercellular-junctional complexes, and cell shape and volume in response to osmotic "],"journal":["The EMBO journal"],"pagination":["1134-45"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC556394"],"repository":["biostudies-literature"],"pubmed_title":["p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP."],"pmcid":["PMC556394"],"pubmed_authors":["Sabio G","Arthur JS","Goedert M","Murray-Tait V","Centeno F","Morrice NA","Cuenda A","Kuma Y","Carr J","Peggie M"],"additional_accession":[]},"is_claimable":false,"name":"p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP.","description":"Activation of the p38 MAP kinase pathways is crucial for the adaptation of mammalian cells to changes in the osmolarity of the environment. Here we identify SAP97/hDlg, the mammalian homologue of the Drosophila tumour suppressor Dlg, as a physiological substrate for the p38gamma MAP kinase (SAPK3/p38gamma) isoform. SAP97/hDlg is a scaffold protein that forms multiprotein complexes with a variety of proteins and is targeted to the cytoskeleton by its association with the protein guanylate kinase-associated protein (GKAP). The SAPK3/p38gamma-catalysed phosphorylation of SAP97/hDlg triggers its dissociation from GKAP and therefore releases it from the cytoskeleton. This is likely to regulate the integrity of intercellular-junctional complexes, and cell shape and volume in response to osmotic ","dates":{"release":"2005-01-01T00:00:00Z","publication":"2005 Mar","modification":"2026-07-15T11:13:56.277Z","creation":"2019-03-27T01:08:42Z"},"accession":"S-EPMC556394","cross_references":{"pubmed":["15729360"],"doi":["10.1038/sj.emboj.7600578"]}}