{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mack NA"],"funding":["Cancer Research UK","Medical Research Council"],"pagination":["1169-80"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3498067"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(11)"],"pubmed_abstract":["Although Rac and its activator Tiam1 are known to stimulate cell-cell adhesion, the mechanisms regulating their activity in cell-cell junction formation are poorly understood. Here, we identify β2-syntrophin as a Tiam1 interactor required for optimal cell-cell adhesion. We show that during tight-junction (TJ) assembly β2-syntrophin promotes Tiam1-Rac activity, in contrast to the function of the apical determinant Par-3 whose inhibition of Tiam1-Rac activity is necessary for TJ assembly. We further demonstrate that β2-syntrophin localizes more basally than Par-3 at cell-cell junctions, thus generating an apicobasal Rac activity gradient at developing cell-cell junctions. Targeting active Rac to TJs shows that this gradient is required for optimal TJ assembly and apical lumen formation. Cons"],"journal":["Nature cell biology"],"pubmed_title":["β2-syntrophin and Par-3 promote an apicobasal Rac activity gradient at cell-cell junctions by differentially regulating Tiam1 activity."],"pmcid":["PMC3498067"],"funding_grant_id":["A5294","12937","MR/J00104X/1","15565"],"pubmed_authors":["Porter AP","Anderson KI","Schwarz JP","Whalley HJ","Jones RC","Bjartell A","Mack NA","Malliri A","Khaja AS"],"additional_accession":[]},"is_claimable":false,"name":"β2-syntrophin and Par-3 promote an apicobasal Rac activity gradient at cell-cell junctions by differentially regulating Tiam1 activity.","description":"Although Rac and its activator Tiam1 are known to stimulate cell-cell adhesion, the mechanisms regulating their activity in cell-cell junction formation are poorly understood. Here, we identify β2-syntrophin as a Tiam1 interactor required for optimal cell-cell adhesion. We show that during tight-junction (TJ) assembly β2-syntrophin promotes Tiam1-Rac activity, in contrast to the function of the apical determinant Par-3 whose inhibition of Tiam1-Rac activity is necessary for TJ assembly. We further demonstrate that β2-syntrophin localizes more basally than Par-3 at cell-cell junctions, thus generating an apicobasal Rac activity gradient at developing cell-cell junctions. Targeting active Rac to TJs shows that this gradient is required for optimal TJ assembly and apical lumen formation. Cons","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Nov","modification":"2025-04-04T01:06:19.27Z","creation":"2019-03-27T01:00:36Z"},"accession":"S-EPMC3498067","cross_references":{"pubmed":["23103911"],"doi":["10.1038/ncb2608"]}}