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| http://purl.uniprot.org/citations/11063739 | http://www.w3.org/2000/01/rdf-schema#comment | "In the present study, we examined the possible interaction between Rab4 and syntaxin 4, both having been implicated in insulin-induced GLUT4 translocation. Rab4 and syntaxin 4 were coimmunoprecipitated from the lysates of electrically permeabilized rat adipocytes. The interaction between the two proteins was reduced by insulin treatment and increased by the addition of guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS). An in vitro binding assay revealed that the bacterially expressed Rab4 was bound to a glutathione S-transferase fusion protein containing the cytoplasmic domain of syntaxin 4 (GST-syntaxin 4-(1-273)) but not to syntaxin 1A or vesicle-associated membrane protein-2. The interaction between Rab4 and syntaxin 4 seemed to be regulated by the guanine nucleotide status of Rab4, because 1) GTPgammaS treatment of the cells significantly increased, but guanosine 5'-O-(2-thiodiphosphate) (GDPbetaS) treatment decreased the amount of Rab4 pulled down with GST-syntaxin 4-(1-273) from the cell lysates; 2) GTPgammaS loading on Rab4 caused a marked increase in the affinity of Rab4 to syntaxin 4 whereas GDPbetaS loading had little effect; and 3) a GTPase-deficient mutant of Rab4 (Rab4(Q67L)), but not a GTP-binding-defective mutant (Rab4(S22N)), was bound to GST-syntaxin 4-(1-273). Although insulin stimulated [gamma-(32)P]GTP binding to Rab4 in a time-dependent fashion, its effect on the Rab4 interaction with syntaxin 4 was apparently biphasic; an initial increase in Rab4 associated with syntaxin 4 was followed by a gradual dissociation of the GTPase from syntaxin 4. Finally, the binding of Rab4(Q67L) to GST-syntaxin 4-(1-273) was inhibited by munc-18c in a dose-dependent manner, indicating that GTP-loaded Rab4 binds to syntaxin 4 in the open conformation. These results suggest that 1) Rab4 interacts with syntaxin 4 in a direct and specific manner, and 2) the interaction is regulated by the guanine nucleotide status of Rab4 as well as by the conformational status of syntaxin 4."xsd:string |
| http://purl.uniprot.org/citations/11063739 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m003883200"xsd:string |
| http://purl.uniprot.org/citations/11063739 | http://purl.uniprot.org/core/author | "Li L."xsd:string |
| http://purl.uniprot.org/citations/11063739 | http://purl.uniprot.org/core/author | "Shibata H."xsd:string |
| http://purl.uniprot.org/citations/11063739 | http://purl.uniprot.org/core/author | "Kojima I."xsd:string |
| http://purl.uniprot.org/citations/11063739 | http://purl.uniprot.org/core/author | "Omata W."xsd:string |
| http://purl.uniprot.org/citations/11063739 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11063739 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/11063739 | http://purl.uniprot.org/core/pages | "5265-5273"xsd:string |
| http://purl.uniprot.org/citations/11063739 | http://purl.uniprot.org/core/title | "Direct interaction of Rab4 with syntaxin 4."xsd:string |
| http://purl.uniprot.org/citations/11063739 | http://purl.uniprot.org/core/volume | "276"xsd:string |
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