Metastasis-associated protein MTA2 is a protein that in humans is encoded by the MTA2 gene.[1][2]
This gene encodes a protein that has been identified as a component of NuRD, a nucleosome remodeling deacetylase complex identified in the nucleus of human cells. It shows a very broad expression pattern and is strongly expressed in many tissues. It may represent one member of a small gene family that encode different but related proteins involved either directly or indirectly in transcriptional regulation. Their indirect effects on transcriptional regulation may include chromatin remodeling. It is closely related to another member of this family, a protein that has been correlated with the metastatic potential of certain carcinomas. These two proteins are so closely related that they share the same types of domains. These domains include two DNA binding domains, a dimerization domain, and a domain commonly found in proteins that methylate DNA. One of the proteins known to be a target protein for this gene product is p53. Deacteylation of p53 is correlated with a loss of growth inhibition in transformed cells supporting a connection between these gene family members and metastasis.[2]
Interactions
MTA2 has been shown to interact with HDAC1,[3][4][5][6] Histone deacetylase 2,[3][5][7] MTA1,[3] CHD4,[3] RBBP7,[3][5] RBBP4,[3][5] MBD3[5][8][9] and SATB1.[6]
References
- ^ Futamura M, Nishimori H, Shiratsuchi T, Saji S, Nakamura Y, Tokino T (Mar 1999). "Molecular cloning, mapping, and characterization of a novel human gene, MTA1-L1, showing homology to a metastasis-associated gene, MTA1". J Hum Genet 44 (1): 52–6. doi:10.1007/s100380050107. PMID 9929979.
- ^ a b "Entrez Gene: MTA2 metastasis associated 1 family, member 2".
- ^ a b c d e f Yao, Ya-Li; Yang Wen-Ming (Oct 2003). "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". J. Biol. Chem. (United States) 278 (43): 42560–8. doi:10.1074/jbc.M302955200. ISSN 0021-9258. PMID 12920132.
- ^ You, A; Tong J K; Grozinger C M; Schreiber S L (Feb 2001). "CoREST is an integral component of the CoREST- human histone deacetylase complex". Proc. Natl. Acad. Sci. U.S.A. (United States) 98 (4): 1454–8. doi:10.1073/pnas.98.4.1454. ISSN 0027-8424. PMC 29278. PMID 11171972.
- ^ a b c d e Zhang, Y; Ng H H; Erdjument-Bromage H; Tempst P; Bird A; Reinberg D (Aug 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. (UNITED STATES) 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. ISSN 0890-9369. PMC 316920. PMID 10444591.
- ^ a b Yasui, Dag; Miyano Masaru, Cai Shutao, Varga-Weisz Patrick, Kohwi-Shigematsu Terumi (Oct 2002). "SATB1 targets chromatin remodelling to regulate genes over long distances". Nature (England) 419 (6907): 641–5. doi:10.1038/nature01084. ISSN 0028-0836. PMID 12374985.
- ^ Hakimi, Mohamed-Ali; Dong Yuanshu; Lane William S; Speicher David W; Shiekhattar Ramin (Feb 2003). "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes". J. Biol. Chem. (United States) 278 (9): 7234–9. doi:10.1074/jbc.M208992200. ISSN 0021-9258. PMID 12493763.
- ^ Sakai, Hirotaka; Urano Takeshi; Ookata Kayoko; Kim Mi-Hyun; Hirai Yugo; Saito Motoki; Nojima Yoshihisa; Ishikawa Fuyuki (Dec 2002). "MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase". J. Biol. Chem. (United States) 277 (50): 48714–23. doi:10.1074/jbc.M208461200. ISSN 0021-9258. PMID 12354758.
- ^ Saito, Motoki; Ishikawa Fuyuki (Sep 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. (United States) 277 (38): 35434–9. doi:10.1074/jbc.M203455200. ISSN 0021-9258. PMID 12124384.
Further reading
- Zhang Y, LeRoy G, Seelig HP et al. (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 et al. (1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex.". Nature 395 (6705): 917–21. doi:10.1038/27699. PMID 9804427.
- Xue Y, Wong J, Moreno GT et al. (1999). "NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities.". Mol. Cell 2 (6): 851–61. doi:10.1016/S1097-2765(00)80299-3. PMID 9885572.
- Zhang Y, Ng HH, Erdjument-Bromage H et al. (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 et al. (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.
- Luo J, Su F, Chen D et al. (2000). "Deacetylation of p53 modulates its effect on cell growth and apoptosis.". Nature 408 (6810): 377–81. doi:10.1038/35042612. PMID 11099047.
- Humphrey GW, Wang Y, Russanova VR et al. (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.
- Feng Q, Zhang Y (2001). "The MeCP1 complex represses transcription through preferential binding, remodeling, and deacetylating methylated nucleosomes.". Genes Dev. 15 (7): 827–32. doi:10.1101/gad.876201. PMC 312663. PMID 11297506.
- Shi Y, Downes M, Xie W et al. (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.
- 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.
- Yasui D, Miyano M, Cai S et al. (2002). "SATB1 targets chromatin remodelling to regulate genes over long distances.". Nature 419 (6907): 641–5. doi:10.1038/nature01084. PMID 12374985.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Hakimi MA, Dong Y, Lane WS et al. (2003). "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes.". J. Biol. Chem. 278 (9): 7234–9. doi:10.1074/jbc.M208992200. PMID 12493763.
- Fujita N, Jaye DL, Kajita M et al. (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.
- Yao YL, Yang WM (2004). "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity.". J. Biol. Chem. 278 (43): 42560–8. doi:10.1074/jbc.M302955200. PMID 12920132.
- Zoltewicz JS, Stewart NJ, Leung R, Peterson AS (2004). "Atrophin 2 recruits histone deacetylase and is required for the function of multiple signaling centers during mouse embryogenesis.". Development 131 (1): 3–14. doi:10.1242/dev.00908. PMID 14645126.
- Miaczynska M, Christoforidis S, Giner A et al. (2004). "APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment.". Cell 116 (3): 445–56. doi:10.1016/S0092-8674(04)00117-5. PMID 15016378.
- Jiang CL, Jin SG, Pfeifer GP (2005). "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.
- Gerhard DS, Wagner L, Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
External links
- MTA2 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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