Proto-oncogene DBL is a protein that in humans is encoded by the MCF2gene.[1][2][3]
MCF2 is a member of a large family of GDP-GTP exchange factors that modulate the activity of small GTPases of the Rho family. Five-prime recombinations result in the loss of N-terminal codons, producing MCF2 variants with oncogenic potential.[supplied by OMIM][3]
References
↑Noguchi T, Galland F, Batoz M, Mattei MG, Birnbaum D (Apr 1994). "Activation of a mcf.2 oncogene by deletion of amino-terminal coding sequences". Oncogene. 3 (6): 709–15. PMID2577874.
↑Galland F, Stefanova M, Lafage M, Birnbaum D (Jul 1992). "Localization of the 5' end of the MCF2 oncogene to human chromosome 15q15----q23". Cytogenet Cell Genet. 60 (2): 114–6. doi:10.1159/000133316. PMID1611909.
Ron D, Zannini M, Lewis M, et al. (1991). "A region of proto-dbl essential for its transforming activity shows sequence similarity to a yeast cell cycle gene, CDC24, and the human breakpoint cluster gene, bcr". New Biol. 3 (4): 372–9. PMID2065022.
Hart MJ, Eva A, Zangrilli D, et al. (1994). "Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product". J. Biol. Chem. 269 (1): 62–5. PMID8276860.
Nishida K, Kaziro Y, Satoh T (1999). "Association of the proto-oncogene product dbl with G protein betagamma subunits". FEBS Lett. 459 (2): 186–90. doi:10.1016/S0014-5793(99)01244-2. PMID10518015.
Kato J, Kaziro Y, Satoh T (2000). "Activation of the guanine nucleotide exchange factor Dbl following ACK1-dependent tyrosine phosphorylation". Biochem. Biophys. Res. Commun. 268 (1): 141–7. doi:10.1006/bbrc.2000.2106. PMID10652228.
Zhu K, Debreceni B, Li R, Zheng Y (2000). "Identification of Rho GTPase-dependent sites in the Dbl homology domain of oncogenic Dbl that are required for transformation". J. Biol. Chem. 275 (34): 25993–6001. doi:10.1074/jbc.M003780200. PMID10854437.
Palmieri G, de Franciscis V, Casamassimi A, et al. (2000). "Human dbl proto-oncogene in 85 kb of xq26, and determination of the transcription initiation site". Gene. 253 (1): 107–15. doi:10.1016/S0378-1119(00)00212-2. PMID10925207.
Jin S, Exton JH (2000). "Activation of RhoA by association of Galpha(13) with Dbl". Biochem. Biophys. Res. Commun. 277 (3): 718–21. doi:10.1006/bbrc.2000.3744. PMID11062019.
Vanni C, Mancini P, Gao Y, et al. (2002). "Regulation of proto-Dbl by intracellular membrane targeting and protein stability". J. Biol. Chem. 277 (22): 19745–53. doi:10.1074/jbc.M111025200. PMID11907027.
Wennerberg K, Ellerbroek SM, Liu RY, et al. (2003). "RhoG signals in parallel with Rac1 and Cdc42". J. Biol. Chem. 277 (49): 47810–7. doi:10.1074/jbc.M203816200. PMID12376551.
Komai K, Okayama R, Kitagawa M, et al. (2003). "Alternative splicing variants of the human DBL (MCF-2) proto-oncogene". Biochem. Biophys. Res. Commun. 299 (3): 455–8. doi:10.1016/S0006-291X(02)02645-1. PMID12445822.
Komai K, Mukae-Sakairi N, Kitagawa M, Shiozawa S (2003). "Characterization of novel splicing variants of the mouse MCF-2 (DBL) proto-oncogene". Biochem. Biophys. Res. Commun. 309 (4): 906–9. doi:10.1016/j.bbrc.2003.08.088. PMID13679059.