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MBD3

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{null|date=May 2011}}

{{Infobox_gene}}

Methyl-CpG-binding domain protein 3 is a protein that in humans is encoded by the MBD3 gene.{{cite journal | vauthors = Hendrich B, Bird A | title = Identification and characterization of a family of mammalian methyl-CpG binding proteins | journal = Molecular and Cellular Biology | volume = 18 | issue = 11 | pages = 6538–47 | date = November 1998 | pmid = 9774669 | pmc = 109239 | doi = 10.1128/mcb.18.11.6538}}{{cite journal | vauthors = Hendrich B, Abbott C, McQueen H, Chambers D, Cross S, Bird A | title = Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes | journal = Mammalian Genome | volume = 10 | issue = 9 | pages = 906–12 | date = September 1999 | pmid = 10441743 | doi = 10.1007/s003359901112 | s2cid = 819148 }}{{cite web | title = Entrez Gene: MBD3 methyl-CpG binding domain protein 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53615}}

Function

DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). However, unlike the other family members, MBD3 is not capable of binding to methylated DNA but instead binds to hydroxymethylated DNA.{{cite journal | vauthors = Yildirim O, Li R, Hung JH, Chen PB, Dong X, Ee LS, Weng Z, Rando OJ, Fazzio TG | title = Mbd3/NURD complex regulates expression of 5-hydroxymethylcytosine marked genes in embryonic stem cells | journal = Cell | volume = 147 | issue = 7 | pages = 1498–510 | date = December 2011 | pmid = 22196727 | pmc = 3252821 | doi = 10.1016/j.cell.2011.11.054 }} The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3. MBD3 is a subunit of the NuRD, a multisubunit complex containing nucleosome remodeling and histone deacetylase activities. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex.

MBD3 also contains the coiled‐coil domain common to all three MBD3 isoforms.{{cite journal | vauthors = Hirasaki M, Ueda A, Asaka MN, Uranishi K, Suzuki A, Kohda M, Mizuno Y, Okazaki Y, Nishimoto M, Sharif J, Koseki H, Okuda A | title = Identification of the Coiled-Coil Domain as an Essential Mbd3 Element for Preserving Lineage Commitment Potential of Embryonic Stem Cells | journal = Stem Cells | volume = 36| issue = 9| date = May 2018 | pmid = 29761578 | doi = 10.1002/stem.2849 | pages=1355–1367| doi-access = free }}

Interactions

MBD3 has been shown to interact with:

  • AURKA,{{cite journal | vauthors = Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F | title = MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase | journal = The Journal of Biological Chemistry | volume = 277 | issue = 50 | pages = 48714–23 | date = December 2002 | pmid = 12354758 | doi = 10.1074/jbc.M208461200 | doi-access = free }}
  • GATAD2B,{{cite journal | vauthors = Brackertz M, Boeke J, Zhang R, Renkawitz R | title = Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 43 | pages = 40958–66 | date = October 2002 | pmid = 12183469 | doi = 10.1074/jbc.M207467200 | doi-access = free }}{{cite journal | vauthors = Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y | title = Identification and functional characterization of the p66/p68 components of the MeCP1 complex | journal = Molecular and Cellular Biology | volume = 22 | issue = 2 | pages = 536–46 | date = January 2002 | pmid = 11756549 | pmc = 139742 | doi = 10.1128/MCB.22.2.536-546.2002 }}
  • HDAC1,{{cite journal | vauthors = Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D | title = Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation | journal = Genes & Development | volume = 13 | issue = 15 | pages = 1924–35 | date = August 1999 | pmid = 10444591 | pmc = 316920 | doi = 10.1101/gad.13.15.1924 }}{{cite journal | vauthors = Saito M, Ishikawa F | title = The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 38 | pages = 35434–9 | date = September 2002 | pmid = 12124384 | doi = 10.1074/jbc.M203455200 | doi-access = free }}
  • MTA2, and
  • MBD2.{{cite journal | vauthors = Jiang CL, Jin SG, Pfeifer GP | title = MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex | journal = The Journal of Biological Chemistry | volume = 279 | issue = 50 | pages = 52456–64 | date = December 2004 | pmid = 15456747 | doi = 10.1074/jbc.M409149200 | doi-access = free }}

References

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Further reading

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  • {{cite journal | vauthors = Shen L, Zhang Y | title = 5-Hydroxymethylcytosine: generation, fate, and genomic distribution | journal = Current Opinion in Cell Biology | volume = 25 | issue = 3 | pages = 289–96 | date = June 2013 | pmid = 23498661 | pmc = 4060438 | doi = 10.1016/j.ceb.2013.02.017 }}
  • {{cite journal | vauthors = Abbott WM, Mellor A, Edwards Y, Feizi T | title = Soluble bovine galactose-binding lectin. cDNA cloning reveals the complete amino acid sequence and an antigenic relationship with the major encephalitogenic domain of myelin basic protein | journal = The Biochemical Journal | volume = 259 | issue = 1 | pages = 283–90 | date = April 1989 | pmid = 2470348 | pmc = 1138502 | doi = 10.1042/bj2590283}}
  • {{cite journal | vauthors = Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D | title = The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities | journal = Cell | volume = 95 | issue = 2 | pages = 279–89 | date = October 1998 | pmid = 9790534 | doi = 10.1016/S0092-8674(00)81758-4 | s2cid = 18786866 | doi-access = free }}
  • {{cite journal | vauthors = Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL | title = Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex | journal = Nature | volume = 395 | issue = 6705 | pages = 917–21 | date = October 1998 | pmid = 9804427 | doi = 10.1038/27699 | bibcode = 1998Natur.395..917T | s2cid = 4355885 }}
  • {{cite journal | vauthors = Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D | title = Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation | journal = Genes & Development | volume = 13 | issue = 15 | pages = 1924–35 | date = August 1999 | pmid = 10444591 | pmc = 316920 | doi = 10.1101/gad.13.15.1924 }}
  • {{cite journal | vauthors = Wade PA, Gegonne A, Jones PL, Ballestar E, Aubry F, Wolffe AP | title = Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation | journal = Nature Genetics | volume = 23 | issue = 1 | pages = 62–6 | date = September 1999 | pmid = 10471500 | doi = 10.1038/12664 | s2cid = 52868103 }}
  • {{cite journal | vauthors = Tatematsu KI, Yamazaki T, Ishikawa F | title = MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase | journal = Genes to Cells | volume = 5 | issue = 8 | pages = 677–88 | date = August 2000 | pmid = 10947852 | doi = 10.1046/j.1365-2443.2000.00359.x | s2cid = 25185979 | doi-access = free }}
  • {{cite journal | vauthors = Humphrey GW, Wang Y, Russanova VR, Hirai T, Qin J, Nakatani Y, Howard BH | title = Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1 | journal = The Journal of Biological Chemistry | volume = 276 | issue = 9 | pages = 6817–24 | date = March 2001 | pmid = 11102443 | doi = 10.1074/jbc.M007372200 | doi-access = free }}
  • {{cite journal | vauthors = Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM | title = Sharp, an inducible cofactor that integrates nuclear receptor repression and activation | journal = Genes & Development | volume = 15 | issue = 9 | pages = 1140–51 | date = May 2001 | pmid = 11331609 | pmc = 312688 | doi = 10.1101/gad.871201 }}
  • {{cite journal | vauthors = Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y | title = Identification and functional characterization of the p66/p68 components of the MeCP1 complex | journal = Molecular and Cellular Biology | volume = 22 | issue = 2 | pages = 536–46 | date = January 2002 | pmid = 11756549 | pmc = 139742 | doi = 10.1128/MCB.22.2.536-546.2002 }}
  • {{cite journal | vauthors = Schlegel J, Güneysu S, Mennel HD | title = Expression of the genes of methyl-binding domain proteins in human gliomas | journal = Oncology Reports | volume = 9 | issue = 2 | pages = 393–5 | year = 2002 | pmid = 11836615 | doi = 10.3892/or.9.2.393 }}
  • {{cite journal | vauthors = Saito M, Ishikawa F | title = The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 38 | pages = 35434–9 | date = September 2002 | pmid = 12124384 | doi = 10.1074/jbc.M203455200 | doi-access = free }}
  • {{cite journal | vauthors = Brackertz M, Boeke J, Zhang R, Renkawitz R | title = Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 43 | pages = 40958–66 | date = October 2002 | pmid = 12183469 | doi = 10.1074/jbc.M207467200 | doi-access = free }}
  • {{cite journal | vauthors = Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F | title = MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase | journal = The Journal of Biological Chemistry | volume = 277 | issue = 50 | pages = 48714–23 | date = December 2002 | pmid = 12354758 | doi = 10.1074/jbc.M208461200 | doi-access = free }}
  • {{cite journal | vauthors = Fujita N, Jaye DL, Kajita M, Geigerman C, Moreno CS, Wade PA | title = MTA3, a Mi-2/NuRD complex subunit, regulates an invasive growth pathway in breast cancer | journal = Cell | volume = 113 | issue = 2 | pages = 207–19 | date = April 2003 | pmid = 12705869 | doi = 10.1016/S0092-8674(03)00234-4 | s2cid = 5773916 | doi-access = free }}
  • {{cite journal | vauthors = Fujita N, Jaye DL, Geigerman C, Akyildiz A, Mooney MR, Boss JM, Wade PA | title = MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation | journal = Cell | volume = 119 | issue = 1 | pages = 75–86 | date = October 2004 | pmid = 15454082 | doi = 10.1016/j.cell.2004.09.014 | s2cid = 17391732 | doi-access = free }}

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Category:Human proteins