MBD3: Difference between revisions
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| | '''Methyl-CpG-binding domain protein 3''' is a [[protein]] that in humans is encoded by the ''MBD3'' [[gene]].<ref name="pmid9774669">{{cite journal | vauthors = Hendrich B, Bird A | title = Identification and characterization of a family of mammalian methyl-CpG binding proteins | journal = Mol Cell Biol | volume = 18 | issue = 11 | pages = 6538–47 | date = Nov 1998 | pmid = 9774669 | pmc = 109239 | doi = }}</ref><ref name="pmid10441743">{{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 = Mamm Genome | volume = 10 | issue = 9 | pages = 906–12 | date = Sep 1999 | pmid = 10441743 | pmc = | doi = 10.1007/s003359901112 }}</ref><ref name="entrez">{{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| accessdate = }}</ref> | ||
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== 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|methyl-CpG binding domain]] (MBD). However, unlike the other family members, MBD3 is not capable of binding to methylated DNA but instead binds to [[5-Hydroxymethylcytosine|hydroxymethylated DNA]] [http://www.sciencedirect.com/science/article/pii/S0092867411014498]. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3. MBD3 is a subunit of the [[Mi-2/NuRD complex|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.<ref name="entrez"/> | |||
==References== | == Interactions == | ||
{{reflist | |||
==Further reading== | MBD3 has been shown to [[Protein-protein interaction|interact]] with: | ||
* [[Aurora A kinase|AURKA]],<ref name = pmid12354758>{{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 = J. Biol. Chem. | volume = 277 | issue = 50 | pages = 48714–23 | year = 2002 | pmid = 12354758 | doi = 10.1074/jbc.M208461200 }}</ref> | |||
* [[GATAD2B]],<ref name = pmid12183469>{{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 = J. Biol. Chem. | volume = 277 | issue = 43 | pages = 40958–66 | year = 2002 | pmid = 12183469 | doi = 10.1074/jbc.M207467200 }}</ref><ref name = pmid11756549>{{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 = Mol. Cell. Biol. | volume = 22 | issue = 2 | pages = 536–46 | year = 2002 | pmid = 11756549 | pmc = 139742 | doi = 10.1128/MCB.22.2.536-546.2002 }}</ref> | |||
* [[HDAC1]],<ref name = pmid12354758/><ref name = pmid10444591>{{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 Dev. | volume = 13 | issue = 15 | pages = 1924–35 | year = 1999 | pmid = 10444591 | pmc = 316920 | doi = 10.1101/gad.13.15.1924 }}</ref><ref name = pmid12124384>{{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 = J. Biol. Chem. | volume = 277 | issue = 38 | pages = 35434–9 | year = 2002 | pmid = 12124384 | doi = 10.1074/jbc.M203455200 }}</ref> | |||
* [[MTA2]],<ref name = pmid12354758/><ref name = pmid10444591/><ref name = pmid12124384/> and | |||
* [[Methyl-CpG-binding domain protein 2|MBD2]].<ref name = pmid10444591/><ref name = pmid15456747>{{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 = J. Biol. Chem. | volume = 279 | issue = 50 | pages = 52456–64 | year = 2004 | pmid = 15456747 | doi = 10.1074/jbc.M409149200 }}</ref> | |||
== References == | |||
{{reflist}} | |||
== Further reading == | |||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{ | * {{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 | year = 2013 | pmid = 23498661 | doi = 10.1016/j.ceb.2013.02.017 | pmc=4060438}} | ||
| | * {{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 = Biochem. J. | volume = 259 | issue = 1 | pages = 283–90 | year = 1989 | pmid = 2470348 | pmc = 1138502 | doi = }} | ||
*{{cite journal | * {{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 | year = 1998 | pmid = 9790534 | doi = 10.1016/S0092-8674(00)81758-4 }} | ||
* {{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 | year = 1998 | pmid = 9804427 | doi = 10.1038/27699 }} | |||
*{{cite journal | * {{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 Dev. | volume = 13 | issue = 15 | pages = 1924–35 | year = 1999 | pmid = 10444591 | pmc = 316920 | doi = 10.1101/gad.13.15.1924 }} | ||
*{{cite journal | * {{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 = Nat. Genet. | volume = 23 | issue = 1 | pages = 62–6 | year = 1999 | pmid = 10471500 | doi = 10.1038/12664 }} | ||
*{{cite journal | * {{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 Cells | volume = 5 | issue = 8 | pages = 677–88 | year = 2000 | pmid = 10947852 | doi = 10.1046/j.1365-2443.2000.00359.x }} | ||
* {{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 = J. Biol. Chem. | volume = 276 | issue = 9 | pages = 6817–24 | year = 2001 | pmid = 11102443 | doi = 10.1074/jbc.M007372200 }} | |||
*{{cite journal | * {{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 Dev. | volume = 15 | issue = 9 | pages = 1140–51 | year = 2001 | pmid = 11331609 | pmc = 312688 | doi = 10.1101/gad.871201 }} | ||
*{{cite journal | * {{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 = Mol. Cell. Biol. | volume = 22 | issue = 2 | pages = 536–46 | year = 2002 | pmid = 11756549 | pmc = 139742 | doi = 10.1128/MCB.22.2.536-546.2002 }} | ||
*{{cite journal | * {{cite journal | vauthors = Schlegel J, Güneysu S, Mennel HD | title = Expression of the genes of methyl-binding domain proteins in human gliomas. | journal = Oncol. Rep. | volume = 9 | issue = 2 | pages = 393–5 | year = 2002 | pmid = 11836615 | doi = 10.3892/or.9.2.393 }} | ||
*{{cite journal | * {{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 = J. Biol. Chem. | volume = 277 | issue = 38 | pages = 35434–9 | year = 2002 | pmid = 12124384 | doi = 10.1074/jbc.M203455200 }} | ||
*{{cite journal | * {{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 = J. Biol. Chem. | volume = 277 | issue = 43 | pages = 40958–66 | year = 2002 | pmid = 12183469 | doi = 10.1074/jbc.M207467200 }} | ||
*{{cite journal | * {{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 = J. Biol. Chem. | volume = 277 | issue = 50 | pages = 48714–23 | year = 2003 | pmid = 12354758 | doi = 10.1074/jbc.M208461200 }} | ||
*{{cite journal | * {{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 | year = 2003 | pmid = 12705869 | doi = 10.1016/S0092-8674(03)00234-4 }} | ||
*{{cite journal | * {{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 | year = 2004 | pmid = 15454082 | doi = 10.1016/j.cell.2004.09.014 }} | ||
*{{cite journal | |||
*{{cite journal | |||
*{{cite journal | |||
}} | |||
{{refend}} | {{refend}} | ||
[[Category:Human proteins]] | |||
Revision as of 06:12, 4 September 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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Methyl-CpG-binding domain protein 3 is a protein that in humans is encoded by the MBD3 gene.[1][2][3]
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 [2]. 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.[3]
Interactions
MBD3 has been shown to interact with:
References
- ↑ Hendrich B, Bird A (Nov 1998). "Identification and characterization of a family of mammalian methyl-CpG binding proteins". Mol Cell Biol. 18 (11): 6538–47. PMC 109239. PMID 9774669.
- ↑ Hendrich B, Abbott C, McQueen H, Chambers D, Cross S, Bird A (Sep 1999). "Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes". Mamm Genome. 10 (9): 906–12. doi:10.1007/s003359901112. PMID 10441743.
- ↑ 3.0 3.1 "Entrez Gene: MBD3 methyl-CpG binding domain protein 3".
- ↑ 4.0 4.1 4.2 Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F (2002). "MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase". J. Biol. Chem. 277 (50): 48714–23. doi:10.1074/jbc.M208461200. PMID 12354758.
- ↑ Brackertz M, Boeke J, Zhang R, Renkawitz R (2002). "Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3". J. Biol. Chem. 277 (43): 40958–66. doi:10.1074/jbc.M207467200. PMID 12183469.
- ↑ Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y (2002). "Identification and functional characterization of the p66/p68 components of the MeCP1 complex". Mol. Cell. Biol. 22 (2): 536–46. doi:10.1128/MCB.22.2.536-546.2002. PMC 139742. PMID 11756549.
- ↑ 7.0 7.1 7.2 Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
- ↑ 8.0 8.1 Saito M, Ishikawa F (2002). "The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2". J. Biol. Chem. 277 (38): 35434–9. doi:10.1074/jbc.M203455200. PMID 12124384.
- ↑ Jiang CL, Jin SG, Pfeifer GP (2004). "MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex". J. Biol. Chem. 279 (50): 52456–64. doi:10.1074/jbc.M409149200. PMID 15456747.
Further reading
- Shen L, Zhang Y (2013). "5-Hydroxymethylcytosine: generation, fate, and genomic distribution". Current Opinion in Cell Biology. 25 (3): 289–96. doi:10.1016/j.ceb.2013.02.017. PMC 4060438. PMID 23498661.
- Abbott WM, Mellor A, Edwards Y, Feizi T (1989). "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". Biochem. J. 259 (1): 283–90. PMC 1138502. PMID 2470348.
- Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D (1998). "The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities". Cell. 95 (2): 279–89. doi:10.1016/S0092-8674(00)81758-4. PMID 9790534.
- Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". Nature. 395 (6705): 917–21. doi:10.1038/27699. PMID 9804427.
- Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
- Wade PA, Gegonne A, Jones PL, Ballestar E, Aubry F, Wolffe AP (1999). "Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation". Nat. Genet. 23 (1): 62–6. doi:10.1038/12664. PMID 10471500.
- Tatematsu KI, Yamazaki T, Ishikawa F (2000). "MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase". Genes Cells. 5 (8): 677–88. doi:10.1046/j.1365-2443.2000.00359.x. PMID 10947852.
- Humphrey GW, Wang Y, Russanova VR, Hirai T, Qin J, Nakatani Y, Howard BH (2001). "Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1". J. Biol. Chem. 276 (9): 6817–24. doi:10.1074/jbc.M007372200. PMID 11102443.
- Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM (2001). "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation". Genes Dev. 15 (9): 1140–51. doi:10.1101/gad.871201. PMC 312688. PMID 11331609.
- Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y (2002). "Identification and functional characterization of the p66/p68 components of the MeCP1 complex". Mol. Cell. Biol. 22 (2): 536–46. doi:10.1128/MCB.22.2.536-546.2002. PMC 139742. PMID 11756549.
- Schlegel J, Güneysu S, Mennel HD (2002). "Expression of the genes of methyl-binding domain proteins in human gliomas". Oncol. Rep. 9 (2): 393–5. doi:10.3892/or.9.2.393. PMID 11836615.
- Saito M, Ishikawa F (2002). "The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2". J. Biol. Chem. 277 (38): 35434–9. doi:10.1074/jbc.M203455200. PMID 12124384.
- Brackertz M, Boeke J, Zhang R, Renkawitz R (2002). "Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3". J. Biol. Chem. 277 (43): 40958–66. doi:10.1074/jbc.M207467200. PMID 12183469.
- Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F (2003). "MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase". J. Biol. Chem. 277 (50): 48714–23. doi:10.1074/jbc.M208461200. PMID 12354758.
- Fujita N, Jaye DL, Kajita M, Geigerman C, Moreno CS, Wade PA (2003). "MTA3, a Mi-2/NuRD complex subunit, regulates an invasive growth pathway in breast cancer". Cell. 113 (2): 207–19. doi:10.1016/S0092-8674(03)00234-4. PMID 12705869.
- Fujita N, Jaye DL, Geigerman C, Akyildiz A, Mooney MR, Boss JM, Wade PA (2004). "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation". Cell. 119 (1): 75–86. doi:10.1016/j.cell.2004.09.014. PMID 15454082.