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http://purl.uniprot.org/citations/12972505http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12972505http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12972505http://www.w3.org/2000/01/rdf-schema#comment"The small GTPase Rab5, which cycles between active (GTP-bound) and inactive (GDP-bound) states, plays essential roles in membrane budding and trafficking in the early endocytic pathway. However, the molecular mechanisms underlying the Rab5-regulated processes are not fully understood other than the targeting event to early endosomes. Here, we report a novel Rab5-binding protein, RIN3, that contains many functional domains shared with other RIN members and additional Pro-rich domains. RIN3 displays the same biochemical properties as RIN2, the stimulator and stabilizer of GTP-Rab5. In addition, RIN3 exhibits its unique intracellular localization. RIN3 expressed in HeLa cells localized to cytoplasmic vesicles and the RIN3-positive vesicles contained Rab5 but not the early endosomal marker EEA1. Transferrin appeared to be transported partly through the RIN3-positive vesicles to early endosomes. RIN3 was also capable of interacting via its Pro-rich domain with amphiphysin II, which contains SH3 domain and participates in receptor-mediated endocytosis. Interestingly, cytoplasmic amphiphysin II was translocated into the RIN3- and Rab5-positive vesicles when co-expressed with RIN3. These results indicate that RIN3 biochemically characterized as the stimulator and stabilizer for GTP-Rab5 plays an important role in the transport pathway from plasma membrane to early endosomes."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.org/dc/terms/identifier"doi:10.1242/jcs.00718"xsd:string
http://purl.uniprot.org/citations/12972505http://purl.org/dc/terms/identifier"doi:10.1242/jcs.00718"xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Saito K."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Saito K."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Araki Y."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Araki Y."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Tsujita K."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Tsujita K."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Katada T."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Katada T."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Kontani K."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Kontani K."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Kajiho H."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Kajiho H."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Kurosu H."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/author"Kurosu H."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/pages"4159-4168"xsd:string
http://purl.uniprot.org/citations/12972505http://purl.uniprot.org/core/pages"4159-4168"xsd:string