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http://purl.uniprot.org/citations/26412237http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26412237http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26412237http://www.w3.org/2000/01/rdf-schema#comment"Adherens junctions (AJs) are membrane-anchored structures composed of E-cadherin and associated proteins, including catenins and actin. The unique plasticity of AJs mediates both the rigidity and flexibility of cell-cell contacts essential for embryonic morphogenesis and adult tissue remodeling. We identified the SUMO protease ULP-2 as a regulator of AJ assembly and show that dysregulated ULP-2 activity impairs epidermal morphogenesis in Caenorhabditis elegans embryos. The conserved cytoplasmic tail of HMR-1/E-cadherin is sumoylated and is a target of ULP-2 desumoylation activity. Coupled sumoylation and desumoylation of HMR-1 are required for its recruitment to the subapical membrane during AJ assembly and the formation of the linkages between AJs and the apical actin cytoskeleton. Sumoylation weakens HMR-1 binding to HMP-2/β-catenin. Our study provides a mechanistic link between the dynamic nature of the SUMO machinery and AJ plasticity and highlight sumoylation as a molecular switch that modulates the binding of E-cadherin to the actin cytoskeleton."xsd:string
http://purl.uniprot.org/citations/26412237http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2015.08.019"xsd:string
http://purl.uniprot.org/citations/26412237http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2015.08.019"xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/author"Broday L."xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/author"Broday L."xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/author"Tsur A."xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/author"Tsur A."xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/author"Bening Abu-Shach U."xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/author"Bening Abu-Shach U."xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/pages"63-77"xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/pages"63-77"xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/title"ULP-2 SUMO Protease Regulates E-Cadherin Recruitment to Adherens Junctions."xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/title"ULP-2 SUMO Protease Regulates E-Cadherin Recruitment to Adherens Junctions."xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/volume"35"xsd:string
http://purl.uniprot.org/citations/26412237http://purl.uniprot.org/core/volume"35"xsd:string
http://purl.uniprot.org/citations/26412237http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26412237
http://purl.uniprot.org/citations/26412237http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26412237
http://purl.uniprot.org/citations/26412237http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26412237
http://purl.uniprot.org/citations/26412237http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26412237