Myb-related protein B is a protein that in humans is encoded by the MYBL2 gene.[1]
The protein encoded by this gene, a member of the MYB family of transcription factor genes, is a nuclear protein involved in cell cycle progression. The encoded protein is phosphorylated by cyclin A/cyclin-dependent kinase 2 during the S-phase of the cell cycle and possesses both activator and repressor activities. It has been shown to activate the cell division cycle 2, cyclin D1, and insulin-like growth factor-binding protein 5 genes. Transcript variants may exist for this gene, but their full-length natures have not been determined.[2]
Interactions
MYBL2 has been shown to interact with Retinoblastoma-like protein 1,[3][4] Cyclin A1,[5] EP300,[6] CREB-binding protein,[7] CDK9,[8] Cyclin-dependent kinase inhibitor 1C[3] and PARP1.[9]
References
- ^ Noben-Trauth K, Copeland NG, Gilbert DJ, Jenkins NA, Sonoda G, Testa JR, Klempnauer KH (December 1996). "Mybl2 (Bmyb) maps to mouse chromosome 2 and human chromosome 20q 13.1". Genomics 35 (3): 610–2. doi:10.1006/geno.1996.0408. PMID 8812502.
- ^ "Entrez Gene: MYBL2 v-myb myeloblastosis viral oncogene homolog (avian)-like 2".
- ^ a b Joaquin, Manel; Watson Roger J (November 2003). "The cell cycle-regulated B-Myb transcription factor overcomes cyclin-dependent kinase inhibitory activity of p57(KIP2) by interacting with its cyclin-binding domain". J. Biol. Chem. (United States) 278 (45): 44255–64. doi:10.1074/jbc.M308953200. ISSN 0021-9258. PMID 12947099.
- ^ Joaquin, Manel; Bessa Maria; Saville Mark K; Watson Roger J (November 2002). "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene (England) 21 (52): 7923–32. doi:10.1038/sj.onc.1206001. ISSN 0950-9232. PMID 12439743.
- ^ Müller-Tidow, C; Wang W, Idos G E, Diederichs S, Yang R, Readhead C, Berdel W E, Serve H, Saville M, Watson R, Koeffler H P (April 2001). "Cyclin A1 directly interacts with B-myb and cyclin A1/cdk2 phosphorylate B-myb at functionally important serine and threonine residues: tissue-specific regulation of B-myb function". Blood (United States) 97 (7): 2091–7. doi:10.1182/blood.V97.7.2091. ISSN 0006-4971. PMID 11264149.
- ^ Johnson, Lance R; Johnson Teresa K; Desler Michelle; Luster Troy A; Nowling Tamara; Lewis Robert E; Rizzino Angie (February 2002). "Effects of B-Myb on gene transcription: phosphorylation-dependent activity ans acetylation by p300". J. Biol. Chem. (United States) 277 (6): 4088–97. doi:10.1074/jbc.M105112200. ISSN 0021-9258. PMID 11733503.
- ^ Bessa, M; Saville M K; Watson R J (June 2001). "Inhibition of cyclin A/Cdk2 phosphorylation impairs B-Myb transactivation function without affecting interactions with DNA or the CBP coactivator". Oncogene (England) 20 (26): 3376–86. doi:10.1038/sj.onc.1204439. ISSN 0950-9232. PMID 11423988.
- ^ De Falco, G; Bagella L; Claudio P P; De Luca A; Fu Y; Calabretta B; Sala A; Giordano A (January 2000). "Physical interaction between CDK9 and B-Myb results in suppression of B-Myb gene autoregulation". Oncogene (ENGLAND) 19 (3): 373–9. doi:10.1038/sj.onc.1203305. ISSN 0950-9232. PMID 10656684.
- ^ Cervellera, M N; Sala A (April 2000). "Poly(ADP-ribose) polymerase is a B-MYB coactivator". J. Biol. Chem. (UNITED STATES) 275 (14): 10692–6. doi:10.1074/jbc.275.14.10692. ISSN 0021-9258. PMID 10744766.
Further reading
- Golay J, Cusmano G, Introna M (1992). "Independent regulation of c-myc, B-myb, and c-myb gene expression by inducers and inhibitors of proliferation in human B lymphocytes.". J. Immunol. 149 (1): 300–8. PMID 1376749.
- Reiss K, Travali S, Calabretta B, Baserga R (1991). "Growth regulated expression of B-myb in fibroblasts and hematopoietic cells.". J. Cell. Physiol. 148 (3): 338–43. doi:10.1002/jcp.1041480303. PMID 1717494.
- Golay J; Capucci A; Arsura M et al. (1991). "Expression of c-myb and B-myb, but not A-myb, correlates with proliferation in human hematopoietic cells". Blood 77 (1): 149–58. PMID 1984793.
- Nomura N; Takahashi M; Matsui M et al. (1989). "Isolation of human cDNA clones of myb-related genes, A-myb and B-myb". Nucleic Acids Res. 16 (23): 11075–89. doi:10.1093/nar/16.23.11075. PMC 338997. PMID 3060855.
- Lam EW, Bennett JD, Watson RJ (1995). "Cell-cycle regulation of human B-myb transcription". Gene 160 (2): 277–81. doi:10.1016/0378-1119(95)00184-8. PMID 7642110.
- Takemoto Y, Tashiro S, Handa H, Ishii S (1994). "Multiple nuclear localization signals of the B-myb gene product". FEBS Lett. 350 (1): 55–60. doi:10.1016/0014-5793(94)00733-0. PMID 8062924.
- Zhou W, Takuwa N, Kumada M, Takuwa Y (1994). "E2F1, B-myb and selective members of cyclin/cdk subunits are targets for protein kinase C-mediated bimodal growth regulation in vascular endothelial cells". Biochem. Biophys. Res. Commun. 199 (1): 191–8. doi:10.1006/bbrc.1994.1213. PMID 8123011.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Arsura M; Luchetti MM; Erba E et al. (1994). "Dissociation between p93B-myb and p75c-myb expression during the proliferation and differentiation of human myeloid cell lines". Blood 83 (7): 1778–90. PMID 8142646.
- Nakagoshi H, Takemoto Y, Ishii S (1993). "Functional domains of the human B-myb gene product". J. Biol. Chem. 268 (19): 14161–7. PMID 8314782.
- Sala A; Kundu M; Casella I et al. (1997). "Activation of human B-MYB by cyclins". Proc. Natl. Acad. Sci. U.S.A. 94 (2): 532–6. doi:10.1073/pnas.94.2.532. PMC 19547. PMID 9012818.
- Suzuki Y; Yoshitomo-Nakagawa K; Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Saville MK, Watson RJ (1998). "The cell-cycle regulated transcription factor B-Myb is phosphorylated by cyclin A/Cdk2 at sites that enhance its transactivation properties". Oncogene 17 (21): 2679–89. doi:10.1038/sj.onc.1202503. PMID 9840932.
- Bartsch O; Horstmann S; Toprak K et al. (1999). "Identification of cyclin A/Cdk2 phosphorylation sites in B-Myb". Eur. J. Biochem. 260 (2): 384–91. doi:10.1046/j.1432-1327.1999.00191.x. PMID 10095772.
- Kim T; Jung H; Min S et al. (1999). "B-myb proto-oncogene products interact in vivo with each other via the carboxy-terminal conserved region". FEBS Lett. 460 (2): 363–8. doi:10.1016/S0014-5793(99)01375-7. PMID 10544265.
- Johnson TK, Schweppe RE, Septer J, Lewis RE (2000). "Phosphorylation of B-Myb regulates its transactivation potential and DNA binding". J. Biol. Chem. 274 (51): 36741–9. doi:10.1074/jbc.274.51.36741. PMID 10593981.
- Horstmann S, Ferrari S, Klempnauer KH (2000). "Regulation of B-Myb activity by cyclin D1". Oncogene 19 (2): 298–306. doi:10.1038/sj.onc.1203302. PMID 10645009.
- De Falco G; Bagella L; Claudio PP et al. (2000). "Physical interaction between CDK9 and B-Myb results in suppression of B-Myb gene autoregulation". Oncogene 19 (3): 373–9. doi:10.1038/sj.onc.1203305. PMID 10656684.
- Cervellera MN, Sala A (2000). "Poly(ADP-ribose) polymerase is a B-MYB coactivator". J. Biol. Chem. 275 (14): 10692–6. doi:10.1074/jbc.275.14.10692. PMID 10744766.
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External links
- MYBL2 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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