Ras-related C3 botulinum toxin substrate 3 is a protein that in humans is encoded by the RAC3gene.[1]
The protein encoded by this gene is a GTPase that belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases.[1]
↑Haataja, Leena; Kaartinen Vesa; Groffen John; Heisterkamp Nora (March 2002). "The small GTPase Rac3 interacts with the integrin-binding protein CIB and promotes integrin alpha(IIb)beta(3)-mediated adhesion and spreading". J. Biol. Chem. United States. 277 (10): 8321–8. doi:10.1074/jbc.M105363200. ISSN0021-9258. PMID11756406. yes
↑Soutoglou, E; Papafotiou G; Katrakili N; Talianidis I (April 2000). "Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins". J. Biol. Chem. UNITED STATES. 275 (17): 12515–20. doi:10.1074/jbc.275.17.12515. ISSN0021-9258. PMID10777539. yes
Further reading
Didsbury J, Weber RF, Bokoch GM, et al. (1989). "rac, a novel ras-related family of proteins that are botulinum toxin substrates". J. Biol. Chem. 264 (28): 16378–82. PMID2674130.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID8889548.
Haataja L, Groffen J, Heisterkamp N (1997). "Characterization of RAC3, a novel member of the Rho family". J. Biol. Chem. 272 (33): 20384–8. doi:10.1074/jbc.272.33.20384. PMID9252344.
Courjal F, Chuchana P, Theillet C, Fort P (1997). "Structure and chromosomal assignment to 22q12 and 17qter of the ras-related Rac2 and Rac3 human genes". Genomics. 44 (2): 242–6. doi:10.1006/geno.1997.4871. PMID9299243.
Soutoglou E, Papafotiou G, Katrakili N, Talianidis I (2000). "Transcriptional activation by hepatocyte nuclear factor-1 requires synergism between multiple coactivator proteins". J. Biol. Chem. 275 (17): 12515–20. doi:10.1074/jbc.275.17.12515. PMID10777539.
Morris CM, Haataja L, McDonald M, et al. (2000). "The small GTPase RAC3 gene is located within chromosome band 17q25.3 outside and telomeric of a region commonly deleted in breast and ovarian tumours". Cytogenet. Cell Genet. 89 (1–2): 18–23. doi:10.1159/000015583. PMID10894930.
Haataja L, Kaartinen V, Groffen J, Heisterkamp N (2002). "The small GTPase Rac3 interacts with the integrin-binding protein CIB and promotes integrin alpha(IIb)beta(3)-mediated adhesion and spreading". J. Biol. Chem. 277 (10): 8321–8. doi:10.1074/jbc.M105363200. PMID11756406.
De Langhe S, Haataja L, Senadheera D, et al. (2002). "Interaction of the small GTPase Rac3 with NRBP, a protein with a kinase-homology domain". Int. J. Mol. Med. 9 (5): 451–9. doi:10.3892/ijmm.9.5.451. PMID11956649.
Zhang A, Yeung PL, Li CW, et al. (2004). "Identification of a novel family of ankyrin repeats containing cofactors for p160 nuclear receptor coactivators". J. Biol. Chem. 279 (32): 33799–805. doi:10.1074/jbc.M403997200. PMID15184363.
Hwang SL, Chang JH, Cheng TS, et al. (2006). "Expression of Rac3 in human brain tumors". Journal of Clinical Neuroscience. 12 (5): 571–4. doi:10.1016/j.jocn.2004.08.013. PMID15993075.
Chan AY, Coniglio SJ, Chuang YY, et al. (2005). "Roles of the Rac1 and Rac3 GTPases in human tumor cell invasion". Oncogene. 24 (53): 7821–9. doi:10.1038/sj.onc.1208909. PMID16027728.
Watabe-Uchida M, John KA, Janas JA, et al. (2006). "The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18". Neuron. 51 (6): 727–39. doi:10.1016/j.neuron.2006.07.020. PMID16982419.
Hajdo-Milasinović A, Ellenbroek SI, van Es S, et al. (2007). "Rac1 and Rac3 have opposing functions in cell adhesion and differentiation of neuronal cells". J. Cell Sci. 120 (Pt 4): 555–66. doi:10.1242/jcs.03364. PMID17244648.