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http://purl.uniprot.org/citations/31402609http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31402609http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31402609http://www.w3.org/2000/01/rdf-schema#comment"S-acylation (palmitoylation) is the only fully reversible lipid modification of proteins; however, little is known about how protein S-acyltransferases (PATs) that mediate it are regulated. DHHC5 is a PAT that is mainly localised at the plasma membrane with roles in synaptic plasticity, massive endocytosis and cancer cell growth/invasion. Here, we demonstrate that DHHC5 binds to and palmitoylates a novel accessory protein Golga7b. Palmitoylation of Golga7b prevents clathrin-mediated endocytosis of DHHC5 and stabilises it at the plasma membrane. Proteomic analysis of the composition of DHHC5/Golga7b-associated protein complexes reveals a striking enrichment in adhesion proteins, particularly components of desmosomes. We show that desmoglein-2 and plakophilin-3 are substrates of DHHC5 and that DHHC5 and Golga7b are required for localisation of desmoglein-2 to the plasma membrane and for desmosomal patterning. Loss of DHHC5/Golga7b causes functional impairments in cell adhesion, suggesting these proteins have a wider role in cell adhesion beyond desmosome assembly. This work uncovers a novel mechanism of DHHC5 regulation by Golga7b and demonstrates a role for the DHHC5/Golga7b complex in the regulation of cell adhesion."xsd:string
http://purl.uniprot.org/citations/31402609http://purl.org/dc/terms/identifier"doi:10.15252/embr.201847472"xsd:string
http://purl.uniprot.org/citations/31402609http://purl.org/dc/terms/identifier"doi:10.15252/embr.201847472"xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/author"Collins M.O."xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/author"Collins M.O."xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/author"Woodley K.T."xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/author"Woodley K.T."xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/name"EMBO Rep."xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/name"EMBO Rep."xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/pages"e47472"xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/pages"e47472"xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/title"S-acylated Golga7b stabilises DHHC5 at the plasma membrane to regulate cell adhesion."xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/title"S-acylated Golga7b stabilises DHHC5 at the plasma membrane to regulate cell adhesion."xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/31402609http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/31402609http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31402609
http://purl.uniprot.org/citations/31402609http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31402609
http://purl.uniprot.org/citations/31402609http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31402609
http://purl.uniprot.org/citations/31402609http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31402609
http://purl.uniprot.org/uniprot/Q9C0B5http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/31402609
http://purl.uniprot.org/uniprot/Q2TAP0http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/31402609