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Gene Review

MBD3  -  methyl-CpG binding domain protein 3

Homo sapiens

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Disease relevance of MBD3

  • Furthermore, silencing of MBD3 by small interfering RNA abrogated the HDI-induced gene regulation and growth inhibition in lung cancer but not in normal cells [1].

High impact information on MBD3


Biological context of MBD3

  • We find that the highly similar MBD2 and MBD3 proteins are encoded by genes that map to different chromosomes in humans and mice but show a similar genomic structure [4].
  • By exploiting this system, we found that MBD3 is phosphorylated in vivo in the late G(2) and early M phases [5].
  • MBD3 was identified as a component of the NuRD/Mi2 complex that shows chromatin remodeling and histone deacetylase activities [6].
  • Transient overexpression of MBD2 suppressed luciferase activity specifically from the methylated rRNA promoter, whereas MBD1 and MBD3 inhibited rRNA promoter activity irrespective of the methylation status [7].
  • Transient transfection of a chimera consisting of a 1072 base pair region extending upstream from the MBD3 initiation codon fused to a luciferase complementary DNA (cDNA) confirmed the presence of a functional promoter unit [8].

Anatomical context of MBD3

  • Interestingly, HDAC1 is distributed at the centrosomes in a manner similar to MBD3 [5].
  • In this study, we stably expressed the FLAG-tagged version of MBD3 in HeLa cells [5].
  • Taken together, these data indicate that a 1072 base pair fragment of the MBD3 promoter is sufficient to drive expression in cell lines and primary cultured neurons, and is able to direct transgene expression in the mouse brain in a pattern with spatial similarity to that of native MBD3 [8].

Associations of MBD3 with chemical compounds


Physical interactions of MBD3

  • The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2 [6].

Other interactions of MBD3

  • MBD2 and MBD3 are two proteins that contain methyl-CpG binding domains and have a transcriptional repression function [3].
  • The data are consistent with a role of MBD3L2 as a transcriptional modulator that can interchange with MBD2 as an MBD3-interacting component of the NuRD complex [3].
  • MBD3L1 interacts with MBD2 and MBD3 in vitro and in yeast two-hybrid assays [9].
  • MBD3 and MBD4/MED1, however, showed a correlation of expression with the grade of malignancy [10].
  • Complex cII (15 S) contained >/=15 proteins, including CHD3/4 (Mi-2), Mta-L1, RbAp48/46, and MBD3, characteristic of vertebrate nucleosome-remodeling complexes [11].

Analytical, diagnostic and therapeutic context of MBD3


  1. Methyl CpG-binding domain protein 3 mediates cancer-selective cytotoxicity by histone deacetylase inhibitors via differential transcriptional reprogramming in lung cancer cells. Noh, E.J., Jang, E.R., Jeong, G., Lee, Y.M., Min, C.K., Lee, J.S. Cancer Res. (2005) [Pubmed]
  2. Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation. Zhang, Y., Ng, H.H., Erdjument-Bromage, H., Tempst, P., Bird, A., Reinberg, D. Genes Dev. (1999) [Pubmed]
  3. MBD3L2 interacts with MBD3 and components of the NuRD complex and can oppose MBD2-MeCP1-mediated methylation silencing. Jin, S.G., Jiang, C.L., Rauch, T., Li, H., Pfeifer, G.P. J. Biol. Chem. (2005) [Pubmed]
  4. Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes. Hendrich, B., Abbott, C., McQueen, H., Chambers, D., Cross, S., Bird, A. Mamm. Genome (1999) [Pubmed]
  5. MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase. Sakai, H., Urano, T., Ookata, K., Kim, M.H., Hirai, Y., Saito, M., Nojima, Y., Ishikawa, F. J. Biol. Chem. (2002) [Pubmed]
  6. The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2. Saito, M., Ishikawa, F. J. Biol. Chem. (2002) [Pubmed]
  7. Role of human ribosomal RNA (rRNA) promoter methylation and of methyl-CpG-binding protein MBD2 in the suppression of rRNA gene expression. Ghoshal, K., Majumder, S., Datta, J., Motiwala, T., Bai, S., Sharma, S.M., Frankel, W., Jacob, S.T. J. Biol. Chem. (2004) [Pubmed]
  8. Identification of a murine methyl cytosine phosphate guanine binding domain-containing factor 3 (MBD3) promoter segment sufficient for driving reporter gene expression in neurons in vitro and in vivo. Jung, B.P., Purushotham, D., Eubanks, J.H. Neuroscience (2007) [Pubmed]
  9. MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex. Jiang, C.L., Jin, S.G., Pfeifer, G.P. J. Biol. Chem. (2004) [Pubmed]
  10. Expression of the genes of methyl-binding domain proteins in human gliomas. Schlegel, J., Güneysu, S., Mennel, H.D. Oncol. Rep. (2002) [Pubmed]
  11. Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1. Humphrey, G.W., Wang, Y., Russanova, V.R., Hirai, T., Qin, J., Nakatani, Y., Howard, B.H. J. Biol. Chem. (2001) [Pubmed]
  12. Methylation mediated silencing of TMS1/ASC gene in prostate cancer. Das, P.M., Ramachandran, K., Vanwert, J., Ferdinand, L., Gopisetty, G., Reis, I.M., Singal, R. Mol. Cancer (2006) [Pubmed]
  13. A novel murine beta -defensin expressed in tongue, esophagus, and trachea. Jia, H.P., Wowk, S.A., Schutte, B.C., Lee, S.K., Vivado, A., Tack, B.F., Bevins, C.L., McCray, P.B. J. Biol. Chem. (2000) [Pubmed]
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