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RAB11FIP3
Introduction
Rab11 family-interacting protein 3 is a protein that in humans is encoded by the RAB11FIP3 gene.[1][2][3]
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][3]
References
References
- β Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Dec 1998). “Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro”. DNA Res. 5 (3): 169β76. doi:10.1093/dnares/5.3.169. PMIDΒ 9734811.
- β Prekeris R, Davies JM, Scheller RH (October 2001). “Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins”. J Biol Chem. 276 (42): 38966β70. doi:10.1074/jbc.M106133200. PMIDΒ 11481332.
- β 3.0 3.1 “Entrez Gene: RAB11FIP3 RAB11 family interacting protein 3 (class II)”.
- β Hales, C M; Griner R; Hobdy-Henderson K C; Dorn M C; Hardy D; Kumar R; Navarre J; Chan E K; Lapierre L A; Goldenring J R (October 2001). “Identification and characterization of a family of Rab11-interacting proteins”. J. Biol. Chem. United States. 276 (42): 39067β75. doi:10.1074/jbc.M104831200. ISSNΒ 0021-9258. PMIDΒ 11495908.
Further reading
Further reading
- Shin OH, Ross AH, Mihai I, Exton JH (2000). “Identification of arfophilin, a target protein for GTP-bound class II ADP-ribosylation factors”. J. Biol. Chem. 274 (51): 36609β15. doi:10.1074/jbc.274.51.36609. PMIDΒ 10593962.
- Daniels RJ, Peden JF, Lloyd C, et al. (2001). “Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16”. Hum. Mol. Genet. 10 (4): 339β52. doi:10.1093/hmg/10.4.339. PMIDΒ 11157797.
- Hales CM, Griner R, Hobdy-Henderson KC, et al. (2001). “Identification and characterization of a family of Rab11-interacting proteins”. J. Biol. Chem. 276 (42): 39067β75. doi:10.1074/jbc.M104831200. PMIDΒ 11495908.
- 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): 10846β52. doi:10.1021/bi0107391. PMIDΒ 11535061.
- 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): 105β10. doi:10.1006/abbi.2002.2778. PMIDΒ 11913976.
- 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): 770β9. doi:10.1016/S0006-291X(02)02720-1. PMIDΒ 12470645.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899β903. Bibcode:2002PNAS…9916899M. doi:10.1073/pnas.242603899. PMCΒ 139241. PMIDΒ 12477932.
- Behrends U, Schneider I, RΓΆssler S, et al. (2003). “Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries”. Int. J. Cancer. 106 (2): 244β51. doi:10.1002/ijc.11208. PMIDΒ 12800201.
- 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): 83β94. doi:10.1016/j.bbrc.2004.04.157. PMIDΒ 15158446.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121β7. doi:10.1101/gr.2596504. PMCΒ 528928. PMIDΒ 15489334.
- Wilson GM, Fielding AB, Simon GC, et al. (2005). “The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis”. Mol. Biol. Cell. 16 (2): 849β60. doi:10.1091/mbc.E04-10-0927. PMCΒ 545916. PMIDΒ 15601896.
- Martin J, Han C, Gordon LA, et al. (2005). “The sequence and analysis of duplication-rich human chromosome 16”. Nature. 432 (7020): 988β94. Bibcode:2004Natur.432..988M. doi:10.1038/nature03187. PMIDΒ 15616553.
- Shiba T, Koga H, Shin HW, et al. (2007). “Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1”. Proc. Natl. Acad. Sci. U.S.A. 103 (42): 15416β21. Bibcode:2006PNAS..10315416S. doi:10.1073/pnas.0605357103. PMCΒ 1622838. PMIDΒ 17030804.
- Horgan CP, Oleksy A, Zhdanov AV, et al. (2007). “Rab11-FIP3 is critical for the structural integrity of the endosomal recycling compartment”. Traffic. 8 (4): 414β30. doi:10.1111/j.1600-0854.2007.00543.x. PMIDΒ 17394487.
- Schonteich E, Pilli M, Simon GC, et al. (2007). “Molecular characterization of Rab11-FIP3 binding to ARF GTPases”. Eur. J. Cell Biol. 86 (8): 417β31. doi:10.1016/j.ejcb.2007.05.004. PMIDΒ 17628206.
