RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/12149250http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12149250http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12149250http://www.w3.org/2000/01/rdf-schema#comment"POB1 was previously identified as a RalBP1-binding protein. POB1 and RalBP1 function downstream of small G protein Ral and regulate receptor-mediated endocytosis. To look for additional functions of POB1, we screened for POB1-binding proteins using a yeast two-hybrid method and found that POB1 interacts with mouse ASAP1, which is a human PAG2 homolog. PAG2 is a paxillin-associated protein with ADP-ribosylation factor GTPase-activating protein activity. POB1 formed a complex with PAG2 in intact cells. The carboxyl-terminal region containing the proline-rich motifs of POB1 directly bound to the carboxyl-terminal region including the SH3 domain of PAG2. Substitutions of Pro(423) and Pro(426) with Ala (POB1(PA)) impaired the binding of POB1 to PAG2. Expression of PAG2 inhibited fibronectin-dependent migration and paxillin recruitment to focal contacts of CHO-IR cells. Co-expression with POB1 but not with POB1(PA) suppressed the inhibitory action of PAG2 on cell migration and paxillin localization. These results suggest that POB1 interacts with PAG2 through its proline-rich motif, thereby regulating cell migration."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m203453200"xsd:string
http://purl.uniprot.org/citations/12149250http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m203453200"xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Kikuchi A."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Kikuchi A."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Kondo A."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Kondo A."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Sabe H."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Sabe H."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Onodera Y."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Onodera Y."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Sugiyama S."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Sugiyama S."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Asahara T."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Asahara T."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Koyama S."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Koyama S."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Oshiro T."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/author"Oshiro T."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12149250http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string