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http://purl.uniprot.org/citations/24338362http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24338362http://www.w3.org/2000/01/rdf-schema#comment"The kinesin motors are important in the regulation of cellular functions such as protein trafficking, spindle organization and centrosome separation. In this study, we have identified POPX2, a serine-threonine phosphatase, as an interacting partner of the KAP3 subunit of the kinesin-2 motor. The kinesin-2 motor is a heterotrimeric complex composed of KIF3A, KIF3B motor subunits and KAP3, the non-motor subunit, which binds the cargo. Here we report that the phosphatase POPX2 is a negative regulator of the trafficking of N-cadherin and other cargoes; consequently, it markedly influences cell-cell adhesion. POPX2 affects trafficking by determining the phosphorylation status of KIF3A at serine 690. This is consistent with the observation that the KIF3A-S690A mutant is defective in cargo trafficking. Our studies also implicate CaMKII as the kinase that phosphorylates KIF3A at serine 690. These results strongly suggest that POPX2 and CaMKII are a phosphatase-kinase pair that regulates kinesin-mediated transport and cell-cell adhesion."xsd:string
http://purl.uniprot.org/citations/24338362http://purl.org/dc/terms/identifier"doi:10.1242/jcs.126482"xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/author"Zeng Y."xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/author"Li H.Y."xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/author"Lai S.K."xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/author"Koh C.G."xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/author"Phang H.Q."xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/author"Chiam K.H."xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/author"Hoon J.L."xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/name"J Cell Sci"xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/pages"727-739"xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/title"POPX2 phosphatase regulates the KIF3 kinesin motor complex."xsd:string
http://purl.uniprot.org/citations/24338362http://purl.uniprot.org/core/volume"127"xsd:string
http://purl.uniprot.org/citations/24338362http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24338362
http://purl.uniprot.org/citations/24338362http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24338362
http://purl.uniprot.org/uniprot/Q02248#attribution-8CEF80501CFB1873A7566B3C6F261AA2http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24338362
http://purl.uniprot.org/uniprot/Q92845#attribution-6D2BCB92BDBB622E6DFF3ED7DCD34561http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24338362
http://purl.uniprot.org/uniprot/Q9Y496#attribution-6D2BCB92BDBB622E6DFF3ED7DCD34561http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24338362
http://purl.uniprot.org/uniprot/Q9Y496#attribution-DCDD5DEB1D710523EBE80442E2F095C9http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24338362
http://purl.uniprot.org/uniprot/P49593#attribution-DCDD5DEB1D710523EBE80442E2F095C9http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24338362
http://purl.uniprot.org/uniprot/#_D3Z7S6-mappedCitation-24338362http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24338362
http://purl.uniprot.org/uniprot/#_D3YYT0-mappedCitation-24338362http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24338362
http://purl.uniprot.org/uniprot/#_D3Z5Q1-mappedCitation-24338362http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24338362