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http://purl.uniprot.org/citations/17030804http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17030804http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17030804http://www.w3.org/2000/01/rdf-schema#comment"Family of Rab11-interacting protein (FIP)3/Arfophlin-1 and FIP4/Arfophilin-2 are dual effectors for Rab11 and ADP ribosylation factor (ARF)5/ARF6, which are involved in membrane delivery from recycling endosomes to the plasma membrane during cytokinesis. Here, we define the distinct C-terminal binding regions of FIP3 and FIP4 for Rab11 and ARF5/ARF6. Furthermore, we determined the crystal structure of Rab11 in complex with the Rab11-binding domain (RBD) of FIP3. The long amphiphilic alpha-helix of FIP3-RBD forms a parallel coiled-coil homodimer, with two symmetric interfaces with two Rab11 molecules. The hydrophobic side of the RBD helix is involved in homodimerization and mediates the interaction with the Rab11 switch 1 region, whereas the opposite hydrophilic side interacts with the Rab11 switch 2 and is the major factor contributing to the binding specificity. The bivalent interaction of FIP3 with Rab11 at the C terminus allows FIP3 to coordinately function with other binding partners, including ARFs."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0605357103"xsd:string
http://purl.uniprot.org/citations/17030804http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0605357103"xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Nakayama K."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Nakayama K."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Koga H."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Koga H."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Shiba T."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Shiba T."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Kato R."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Kato R."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Wakatsuki S."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Wakatsuki S."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Kawasaki M."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Kawasaki M."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Shin H.-W."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/author"Shin H.-W."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/pages"15416-15421"xsd:string
http://purl.uniprot.org/citations/17030804http://purl.uniprot.org/core/pages"15416-15421"xsd:string