Rab11 family-interacting protein 3 is a protein that in humans is encoded by the RAB11FIP3gene.[5][6][7]
Proteins of the large Rab GTPase family (see RAB1A; MIM 179508) have regulatory roles in the formation, targeting, and fusion of intracellular transport vesicles. RAB11FIP3 is one of many proteins that interact with and regulate Rab GTPases (Hales et al., 2001).[supplied by OMIM][7]
Interactions[]
RAB11FIP3 has been shown to interact with RAB11A.[8]
Shin OH, Couvillon AD, Exton JH (2001). "Arfophilin is a common target of both class II and class III ADP-ribosylation factors". Biochemistry. 40 (36): 10846–52. doi:10.1021/bi0107391. PMID11535061.
Yang CS, Weiner H (2002). "Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol". Arch. Biochem. Biophys. 400 (1): 105–10. doi:10.1006/abbi.2002.2778. PMID11913976.
Wallace DM, Lindsay AJ, Hendrick AG, McCaffrey MW (2003). "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells". Biochem. Biophys. Res. Commun. 299 (5): 770–9. doi:10.1016/S0006-291X(02)02720-1. PMID12470645.
Horgan CP, Walsh M, Zurawski TH, McCaffrey MW (2004). "Rab11-FIP3 localises to a Rab11-positive pericentrosomal compartment during interphase and to the cleavage furrow during cytokinesis". Biochem. Biophys. Res. Commun. 319 (1): 83–94. doi:10.1016/j.bbrc.2004.04.157. PMID15158446.
Schonteich E, Pilli M, Simon GC, et al. (2007). "Molecular characterization of Rab11-FIP3 binding to ARF GTPases". Eur. J. Cell Biol. 86 (8): 417–31. doi:10.1016/j.ejcb.2007.05.004. PMID17628206.
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PDB gallery
2d7c: Crystal structure of human Rab11 in complex with FIP3 Rab-binding domain
2hv8: Crystal structure of GTP-bound Rab11 in complex with FIP3
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