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Review

Lysine-specific demethylase 1 as a potential therapeutic target

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Pages 809-820 | Published online: 15 May 2007

Bibliography

  • LUGER K: Structure and dynamic behavior of nucleosomes. Curr. Opin. Genet. Dev. (2003) 13(2):127-135.
  • SCHALCH T, DUDA S, SARGENT DF, RICHMOND TJ: X-ray structure of a tetranucleosome and its implications for the chromatin fibre. Nature (2005) 436(7047):138-141.
  • STRAHL BD, ALLIS CD: The language of covalent histone modifications. Nature (2000) 403(6765):41-45.
  • JENUWEIN T, ALLIS CD: Translating the histone code. Science (2001) 293(5532):1074-1080.
  • SPOTSWOOD HT, TURNER BM: An increasingly complex code. J. Clin. Invest. (2002) 110(5):577-582.
  • TURNER BM: Cellular memory and the histone code. Cell (2002) 111(3):285-291.
  • TAMKUN JW, DEURING R, SCOTT MP et al.: brahma: a regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2/SWI2. Cell (1992) 68(3):561-572.
  • HAYNES SR, DOLLARD C, WINSTON F et al.: The bromodomain: a conserved sequence found in human, Drosophila and yeast proteins. Nucleic Acids Res. (1992) 20(10):2603.
  • ZENG L, ZHOU MM: Bromodomain: an acetyl-lysine binding domain. FEBS Lett. (2002) 513(1):124-128.
  • DHALLUIN C, CARLSON JE, ZENG L et al.: Structure and ligand of a histone acetyltransferase bromodomain. Nature (1999) 399(6735):491-496.
  • JACOBSON RH, LADURNER AG, KING DS, TJIAN R: Structure and function of a human TAFII250 double bromodomain module. Science (2000) 288(5470):1422-1425.
  • PARO R, HOGNESS DS: The Polycomb protein shares a homologous domain with a heterochromatin-associated protein of Drosophila. Proc. Natl. Acad. Sci. USA (1991) 88(1):263-267.
  • EISSENBERG JC: Molecular biology of the chromo domain: an ancient chromatin module comes of age. Gene (2001) 275(1):19-29.
  • BANNISTER AJ, ZEGERMAN P, PARTRIDGE JF et al.: Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature (2001) 410(6824):120-124.
  • LACHNER M, O’CARROLL D, REA S et al.: Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature (2001) 410(6824):116-120.
  • FLANAGAN JF, MI LZ, CHRUSZCZ M et al.: Double chromodomains cooperate to recognize the methylated histone H3 tail. Nature (2005) 438(7071):1181-1185.
  • HUANG Y, FANG J, BEDFORD MT et al.: Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science (2006) 312(5774):748-751.
  • KIM J, DANIEL J, ESPEJO A et al.: Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep. (2006) 7(4):397-403.
  • COTE J, RICHARD S: Tudor domains bind symmetrical dimethylated arginines. J. Biol. Chem. (2005) 280(31):28476-83.
  • WYSOCKA J, SWIGUT T, XIAO H et al.: A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature (2006) 442(7098):86-90.
  • DOYON Y, CAYROU C, ULLAH M et al.: ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol. Cell. (2006) 21(1):51-64.
  • SHI X, HONG T, WALTER KL, EWALT M et al.: ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature (2006) 442(7098):96-99.
  • AASLAND R, STEWART AF, GIBSON T: The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB. Trends Biochem. Sci. (1996) 21(3):87-88.
  • BOYER LA, LATEK RR, PETERSON CL: The SANT domain: a unique histone-tail-binding module? Nat. Rev. Mol. Cell. Biol. (2004) 5(2):158-163.
  • YU J, LI Y, ISHIZUKA T et al.: A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation. EMBO J. (2003) 22(13):3403-3410.
  • ZHANG Y, REINBERG D: Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev. (2001) 15(18):2343-2360.
  • BANNISTER AJ, SCHNEIDER R, KOUZARIDES T: Histone methylation: dynamic or static? Cell (2002) 109(7):801-806.
  • LACHNER M, O’SULLIVAN RJ, JENUWEIN T: An epigenetic road map for histone lysine methylation. J. Cell Sci. (2003) 116(Pt. 11):2117-2124.
  • BAUER UM, DAUJAT S, NIELSEN SJ et al.: Methylation at arginine 17 of histone H3 is linked to gene activation. EMBO Rep. (2002) 3(1):39-44.
  • CHEN D, MA H, HONG H et al.: Regulation of transcription by a protein methyltransferase. Science (1999) 284(5423):2174-2177.
  • STRAHL BD, BRIGGS SD, BRAME CJ et al.: Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1. Curr. Biol. (2001) 11(12):996-1000.
  • WANG H, HUANG ZQ, XIA L et al.: Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor. Science (2001) 293(5531):853-857.
  • CHENG X, COLLINS RE, ZHANG X: Structural and sequence motifs of protein (histone) methylation enzymes. Ann. Rev. Biophys. Biomol. Struct. (2005) 34:267-294.
  • WANG Y, WYSOCKA J, SAYEGH J et al.: Human PAD4 regulates histone arginine methylation levels via demethylimination. Science (2004) 306(5694):279-283.
  • SHI Y, LAN F, MATSON C, MULLIGAN P et al.: Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell (2004) 119(7):941-953.
  • YOU A, TONG JK, GROZINGER CM, SCHREIBER SL: CoREST is an integral component of the CoREST- human histone deacetylase complex. Proc. Natl. Acad. Sci. USA (2001) 98(4):1454-1458.
  • HUMPHREY GW, WANG Y, RUSSANOVA VR et al.: Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1. J. Biol. Chem. (2001) 276(9):6817-6824.
  • BALLAS N, BATTAGLIOLI E, ATOUF F et al.: Regulation of neuronal traits by a novel transcriptional complex. Neuron (2001) 31(3):353-365.
  • HAKIMI MA, BOCHAR DA, CHENOWETH J et al.: A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes. Proc. Natl. Acad. Sci. USA (2002) 99(11):7420-7425.
  • SHI Y, SAWADA J, SUI G et al.: Coordinated histone modifications mediated by a CtBP co-repressor complex. Nature (2003) 422(6933):735-738.
  • FORNERIS F, BINDA C, VANONI MA et al.: Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process. FEBS Lett. (2005) 10:2203-2207.
  • KUBICEK S, JENUWEIN T: A crack in histone lysine methylation. Cell (2004) 19(7):903-906.
  • TSUKADA Y, FANG J, ERDJUMENT-BROMAGE H et al.: Histone demethylation by a family of JmjC domain-containing proteins. Nature (2006) 439(7078):811-816.
  • CHEN Z, ZANG J, WHETSTINE J et al.: Structural insights into histone demethylation by JMJD2 family members. Cell (2006) 125(4):691-702.
  • HAUSINGER RP: FeII/alpha-ketoglutarate-dependent hydroxylases and related enzymes. Crit. Rev. Biochem. Mol. Biol. (2004) 39(1):21-68.
  • KLOSE RJ, KALLIN EM, ZHANG Y: JmjC-domain-containing proteins and histone demethylation. Nat. Rev. Genet. (2006) 7(9):715-727.
  • YAMANE K, TOUMAZOU C, TSUKADA Y et al.: JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. Cell (2006) 125(3):483-495.
  • WHETSTINE JR, NOTTKE A, LAN F et al.: Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell (2006) 125(3):467-481.
  • FODOR BD, KUBICEK S, YONEZAWA M et al.: Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cells. Genes Dev. (2006) 20(12):1557-1562.
  • CHRISTENSEN J, AGGER K, CLOOS PA et al.: RBP2 belongs to a family of demethylases, specific for tri- and dimethylated lysine 4 on histone 3. Cell (2007) 128(6):1063-1076.
  • SEWARD DJ, CUBBERLEY G, KIM S et al.: Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins. Nat. Struct. Mol. Biol. (2007) 14(3):240-242.
  • SHI YJ, MATSON C, LAN F et al.: Regulation of LSD1 histone demethylase activity by its associated factors. Mol. Cell. (2005) 19(6):857-864.
  • LEE MG, WYNDER C, COOCH N, SHIEKHATTAR R: An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation. Nature (2005) 437(7057):432-435.
  • STAVROPOULOS P, BLOBEL G, HOELZ A: Crystal structure and mechanism of human lysine-specific demethylase-1. Nat. Struct. Mol. Biol. (2006) 13(7):626-632.
  • DING Z, GILLESPIE LL, PATERNO GD: Human MI-ER1α and β function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain. Mol. Cell. Biol. (2003) 23(1):250-258.
  • WANG L, RAJAN H, PITMAN JL, MCKEOWN M, TSAI CC: Histone deacetylase-associating Atrophin proteins are nuclear receptor corepressors. Genes Dev. (2006) 20(5):525-530.
  • BOYER LA, LATEK RR, PETERSON CL: The SANT domain: a unique histone-tail-binding module? Nat. Rev. Mol. Cell. Biol. (2004) 5(2):158-163.
  • BOYER LA, LANGER MR, CROWLEY KA et al.: Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes. Mol. Cell. (2002) 10(4):935-942.
  • YANG M, GOCKE CB, LUO X et al.: Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase. Mol. Cell. (2006) 23(3):377-387.
  • METZGER E, WISSMANN M, YIN N et al.: LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature (2005) 437(7057):436-439.
  • ARAVIND L, IYER LM: The SWIRM domain: a conserved module found in chromosomal proteins points to novel chromatin-modifying activities. Genome Biol. (2002) 3(8):RESEARCH0039.
  • FORNERIS F, BINDA C, VANONI MA et al.: Human histone demethylase LSD1 reads the histone code. J. Biol. Chem. (2005) 280(50):41360-41365.
  • BINDA C, MATTEVI A, EDMONDSON DE: Structure-function relationships in flavoenzyme-dependent amine oxidations: a comparison of polyamine oxidase and monoamine oxidase. J. Biol. Chem. (2002) 277(27):23973-23976.
  • LEE MG, WYNDER C, BOCHAR DA et al.: Functional interplay between histone demethylase and deacetylase enzymes. Mol. Cell. Biol. (2006) 26(17):6395-402.
  • YOUDIM MB, EDMONDSON D, TIPTON KF: The therapeutic potential of monoamine oxidase inhibitors. Nat. Rev. Neurosci. (2006) 7(4):295-309.
  • LEE MG, WYNDER C, SCHMIDT DM et al.: Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications. Chem. Biol. (2006) 13(6):563-567.
  • CULHANE JC, SZEWCZUK LM, LIU X et al.: A mechanism-based inactivator for histone demethylase LSD1. J. Am. Chem. Soc. (2006) 128(14):4536-4537.
  • BOLDEN JE, PEART MJ, JOHNSTONE RW: Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov. (2006) 5(9):769-784.
  • SCHNEIDER R, BANNISTER AJ, KOUZARIDES T: Unsafe SETs: histone lysine methyltransferases and cancer. Trends Biochem Sci. (2002) 27(8):396-402.

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