HTATIP
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HTATIP, histonska acetiltransferaza KAT5, je enzim koji je kod čoveka kodiran KAT5 genom.[1][2]
Protein kodiran ovim genom pripada MYST familiji histonskih acetil transferaza (HAT). On je bio originalno izolovan kao HIV-1 TAT-interaktivni protein. HAT proteini učestvuju u regulaciji hromatinskog remodelovanja, transkripciji i drugim nuklearnim procesima putem acetilacije histona i nehistonskih proteina. Ovaj protein je histonska acetilaza koja učestvuje u DNK popravci i apoptozi, i za nju se smatra da ima ulogu u prenosu signala. Alternativno splajsovanje ovog gena rezultuje u višestrukim transkriptnim varijantama.[2]
Interakcije[uredi | uredi kod]
Za HTATIP je bilo pokazano da interaguje sa HDAC7A,[3] FANCD2,[4] CREB1,[5] ETV6,[6] Mdm2,[7] Myc,[8] BCL3,[9] androgenskim receptorom,[10] endotelinskim receptorom tipa A[11] i PLA2G4A.[12]
Reference[uredi | uredi kod]
- ↑ Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G (May 1996). „Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator”. Virology 216 (2): 357–66. DOI:10.1006/viro.1996.0071. PMID 8607265.
- ↑ 2,0 2,1 „Entrez Gene: HTATIP HIV-1 Tat interacting protein, 60kDa”.
- ↑ Xiao, Hui; Chung Jin, Kao Hung-Ying, Yang Yu-Chung (March 2003). „Tip60 is a co-repressor for STAT3”. J. Biol. Chem. (United States) 278 (13): 11197–204. DOI:10.1074/jbc.M210816200. ISSN 0021-9258. PMID 12551922.
- ↑ Hejna, James; Holtorf Megan, Hines Jennie, Mathewson Lauren, Hemphill Aaron, Al-Dhalimy Muhsen, Olson Susan B, Moses Robb E (April 2008). „Tip60 is required for DNA interstrand cross-link repair in the Fanconi anemia pathway”. J. Biol. Chem. (United States) 283 (15): 9844–51. DOI:10.1074/jbc.M709076200. ISSN 0021-9258. PMC 2398728. PMID 18263878.
- ↑ Gavaravarapu, S; Kamine J (March 2000). „Tip60 inhibits activation of CREB protein by protein kinase A”. Biochem. Biophys. Res. Commun. (UNITED STATES) 269 (3): 758–66. DOI:10.1006/bbrc.2000.2358. ISSN 0006-291X. PMID 10720489.
- ↑ Nordentoft, Iver; Jørgensen Poul (August 2003). „The acetyltransferase 60 kDa trans-acting regulatory protein of HIV type 1-interacting protein (Tip60) interacts with the translocation E26 transforming-specific leukaemia gene (TEL) and functions as a transcriptional co-repressor”. Biochem. J. (England) 374 (Pt 1): 165–73. DOI:10.1042/BJ20030087. ISSN 0264-6021. PMC 1223570. PMID 12737628.
- ↑ Legube, Gaëlle; Linares Laetitia K, Lemercier Claudie, Scheffner Martin, Khochbin Saadi, Trouche Didier (April 2002). „Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation”. EMBO J. (England) 21 (7): 1704–12. DOI:10.1093/emboj/21.7.1704. ISSN 0261-4189. PMC 125958. PMID 11927554.
- ↑ Frank, Scott R; Parisi Tiziana, Taubert Stefan, Fernandez Paula, Fuchs Miriam, Chan Ho-Man, Livingston David M, Amati Bruno (June 2003). „MYC recruits the TIP60 histone acetyltransferase complex to chromatin”. EMBO Rep. (England) 4 (6): 575–80. DOI:10.1038/sj.embor.embor861. ISSN 1469-221X. PMC 1319201. PMID 12776177.
- ↑ Dechend, R; Hirano F, Lehmann K, Heissmeyer V, Ansieau S, Wulczyn F G, Scheidereit C, Leutz A (June 1999). „The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators”. Oncogene (ENGLAND) 18 (22): 3316–23. DOI:10.1038/sj.onc.1202717. ISSN 0950-9232. PMID 10362352.
- ↑ Gaughan, Luke; Logan Ian R, Cook Susan, Neal David E, Robson Craig N (July 2002). „Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor”. J. Biol. Chem. (United States) 277 (29): 25904–13. DOI:10.1074/jbc.M203423200. ISSN 0021-9258. PMID 11994312.
- ↑ Lee, H J; Chun M, Kandror K V (May 2001). „Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling”. J. Biol. Chem. (United States) 276 (20): 16597–600. DOI:10.1074/jbc.C000909200. ISSN 0021-9258. PMID 11262386.
- ↑ Sheridan, A M; Force T, Yoon H J, O'Leary E, Choukroun G, Taheri M R, Bonventre J V (July 2001). „PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production”. Mol. Cell. Biol. (United States) 21 (14): 4470–81. DOI:10.1128/MCB.21.14.4470-4481.2001. ISSN 0270-7306. PMC 87107. PMID 11416127.
Literatura[uredi | uredi kod]
- Doyon Y, Côté J (2004). „The highly conserved and multifunctional NuA4 HAT complex.”. Curr. Opin. Genet. Dev. 14 (2): 147–54. DOI:10.1016/j.gde.2004.02.009. PMID 15196461.
- Sapountzi V, Logan IR, Robson CN (2006). „Cellular functions of TIP60.”. Int. J. Biochem. Cell Biol. 38 (9): 1496–509. DOI:10.1016/j.biocel.2006.03.003. PMID 16698308.
- 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.
- 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.
- Yamamoto T, Horikoshi M (1998). „Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60.”. J. Biol. Chem. 272 (49): 30595–8. DOI:10.1074/jbc.272.49.30595. PMID 9388189.
- Kimura A, Horikoshi M (1999). „Tip60 acetylates six lysines of a specific class in core histones in vitro.”. Genes Cells 3 (12): 789–800. DOI:10.1046/j.1365-2443.1998.00229.x. PMID 10096020.
- Dechend R, Hirano F, Lehmann K, et al. (1999). „The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators.”. Oncogene 18 (22): 3316–23. DOI:10.1038/sj.onc.1202717. PMID 10362352.
- Brady ME, Ozanne DM, Gaughan L, et al. (1999). „Tip60 is a nuclear hormone receptor coactivator.”. J. Biol. Chem. 274 (25): 17599–604. DOI:10.1074/jbc.274.25.17599. PMID 10364196.
- Creaven M, Hans F, Mutskov V, et al. (1999). „Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein, Tat.”. Biochemistry 38 (27): 8826–30. DOI:10.1021/bi9907274. PMID 10393559.
- Sliva D, Zhu YX, Tsai S, et al. (1999). „Tip60 interacts with human interleukin-9 receptor alpha-chain.”. Biochem. Biophys. Res. Commun. 263 (1): 149–55. DOI:10.1006/bbrc.1999.1083. PMID 10486269.
- Gavaravarapu S, Kamine J (2000). „Tip60 inhibits activation of CREB protein by protein kinase A.”. Biochem. Biophys. Res. Commun. 269 (3): 758–66. DOI:10.1006/bbrc.2000.2358. PMID 10720489.
- Husi H, Ward MA, Choudhary JS, et al. (2000). „Proteomic analysis of NMDA receptor-adhesion protein signaling complexes.”. Nat. Neurosci. 3 (7): 661–9. DOI:10.1038/76615. PMID 10862698.
- Ikura T, Ogryzko VV, Grigoriev M, et al. (2000). „Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis.”. Cell 102 (4): 463–73. DOI:10.1016/S0092-8674(00)00051-9. PMID 10966108.
- Ran Q, Pereira-Smith OM (2001). „Identification of an alternatively spliced form of the Tat interactive protein (Tip60), Tip60(beta).”. Gene 258 (1-2): 141–6. DOI:10.1016/S0378-1119(00)00410-8. PMID 11111051.
- Lee HJ, Chun M, Kandror KV (2001). „Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling.”. J. Biol. Chem. 276 (20): 16597–600. DOI:10.1074/jbc.C000909200. PMID 11262386.
- Hlubek F, Löhberg C, Meiler J, et al. (2001). „Tip60 is a cell-type-specific transcriptional regulator.”. J. Biochem. 129 (4): 635–41. PMID 11275565.
- Sheridan AM, Force T, Yoon HJ, et al. (2001). „PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production.”. Mol. Cell. Biol. 21 (14): 4470–81. DOI:10.1128/MCB.21.14.4470-4481.2001. PMC 87107. PMID 11416127.
- Cao X, Südhof TC (2001). „A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60.”. Science 293 (5527): 115–20. DOI:10.1126/science.1058783. PMID 11441186.
- Legube G, Linares LK, Lemercier C, et al. (2002). „Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation.”. EMBO J. 21 (7): 1704–12. DOI:10.1093/emboj/21.7.1704. PMC 125958. PMID 11927554.
