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Volumn 11, Issue 5, 2007, Pages 561-568

LSD1 and the chemistry of histone demethylation

Author keywords

[No Author keywords available]

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); HISTONE; HISTONE DEACETYLASE INHIBITOR; HISTONE H3; IRON; METHYLTRANSFERASE; NON HEME IRON DEPENDENT HISTONE DEMETHYLASE JMJC; PROTEIN LSD1; SMALL MOLECULE TRANSPORT AGENT; TRANYLCYPROMINE; UNCLASSIFIED DRUG;

EID: 35348812522     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2007.07.014     Document Type: Review
Times cited : (126)

References (51)
  • 1
    • 0035895525 scopus 로고    scopus 로고
    • The human genome and our view of ourselves
    • Paabo S. The human genome and our view of ourselves. Science 291 (2001) 1219-1220
    • (2001) Science , vol.291 , pp. 1219-1220
    • Paabo, S.1
  • 2
    • 35348833068 scopus 로고    scopus 로고
    • Walsh CT: Posttranslational modification of proteins: expanding nature's inventory. B. Roberts, Colorado; 2005.
  • 3
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., and Allis C.D. Translating the histone code. Science 293 (2001) 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 4
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey V.G., Faulkner R., and Mirsky A.G. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci USA 51 (1964) 786-794
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.G.3
  • 5
    • 0029984469 scopus 로고    scopus 로고
    • Tetrehymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell J.E., Zhou J., Ranalli T., Kobayashi R., Edmondson D.G., Roth S.Y., and Allis C.D. Tetrehymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84 (1996) 843-851
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 6
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast regulator Rpd3p
    • Taunton J., Hassig C.A., and Schreiber S.L. A mammalian histone deacetylase related to the yeast regulator Rpd3p. Science 272 (1996) 408-411
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 8
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • This study identifies for the first time an enzyme responsible for enzymatic protein demethylation.
    • Shi Y., Lan F., Matson C., Mulligan P., Whetstine J.R., Cole P.A., Casero R.A., and Shi Y. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119 (2004) 941-953. This study identifies for the first time an enzyme responsible for enzymatic protein demethylation.
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7    Shi, Y.8
  • 9
    • 0035371872 scopus 로고    scopus 로고
    • Re-SET-ting heterochromatin by histone methyltransferases
    • Jenuwein T. Re-SET-ting heterochromatin by histone methyltransferases. Trends Cell Biol 11 (2001) 266-273
    • (2001) Trends Cell Biol , vol.11 , pp. 266-273
    • Jenuwein, T.1
  • 10
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen F., Gafken P.R., and Gottschling D.E. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 109 (2002) 745-756
    • (2002) Cell , vol.109 , pp. 745-756
    • van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 11
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y., and Struhl K. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev 16 (2002) 1518-1527
    • (2002) Genes Dev , vol.16 , pp. 1518-1527
    • Ng, H.H.1    Feng, Q.2    Wang, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6    Struhl, K.7
  • 12
    • 0037163016 scopus 로고    scopus 로고
    • Disruptor of telomeric silencing 1 is a chromatin-specific histone H3 methyltransferase
    • Lacoste N., Utley R.T., Hunter J., Poirier G.G., and Cote J. Disruptor of telomeric silencing 1 is a chromatin-specific histone H3 methyltransferase. J Biol Chem 277 (2002) 30421-30424
    • (2002) J Biol Chem , vol.277 , pp. 30421-30424
    • Lacoste, N.1    Utley, R.T.2    Hunter, J.3    Poirier, G.G.4    Cote, J.5
  • 13
    • 0015912073 scopus 로고
    • Enzymatic demethylation of calf thymus histones
    • Paik W.K., and Kim S. Enzymatic demethylation of calf thymus histones. Biochem Biophys Res Commun 51 (1973) 781-788
    • (1973) Biochem Biophys Res Commun , vol.51 , pp. 781-788
    • Paik, W.K.1    Kim, S.2
  • 15
    • 33646138230 scopus 로고    scopus 로고
    • JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor
    • Yamane K., Toumazou C., Tsukada Y., Erdjument-Bromage H., Tempst P., Wong J., and Zhang Y. JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. Cell 125 (2006) 483-495
    • (2006) Cell , vol.125 , pp. 483-495
    • Yamane, K.1    Toumazou, C.2    Tsukada, Y.3    Erdjument-Bromage, H.4    Tempst, P.5    Wong, J.6    Zhang, Y.7
  • 16
  • 20
    • 33846132573 scopus 로고    scopus 로고
    • Diversity within the JMJD2 histone demethylase family
    • Shin S., and Janknecht R. Diversity within the JMJD2 histone demethylase family. Biochem Biophys Res Commun 353 (2007) 973-977
    • (2007) Biochem Biophys Res Commun , vol.353 , pp. 973-977
    • Shin, S.1    Janknecht, R.2
  • 24
    • 33847383585 scopus 로고    scopus 로고
    • Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein
    • Lee M.G., Norman J., Shilatifard A., and Shiekhattar R. Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein. Cell 128 (2007) 877-887
    • (2007) Cell , vol.128 , pp. 877-887
    • Lee, M.G.1    Norman, J.2    Shilatifard, A.3    Shiekhattar, R.4
  • 25
    • 34250203607 scopus 로고    scopus 로고
    • Mechanistic analysis of a suicide inactivator of histone demethylase LSD1
    • Szewczuk L.M., Culhane J.C., Yang M., Majumdar A., Yu H., and Cole P.A. Mechanistic analysis of a suicide inactivator of histone demethylase LSD1. Biochemistry 46 (2007) 6892-6902
    • (2007) Biochemistry , vol.46 , pp. 6892-6902
    • Szewczuk, L.M.1    Culhane, J.C.2    Yang, M.3    Majumdar, A.4    Yu, H.5    Cole, P.A.6
  • 26
    • 33144483781 scopus 로고    scopus 로고
    • Structure and function of the SWIRM domain, a conserved protein module found in chromatin regulatory complexes
    • Da G., Lenkart J., Zhao K., Shiekhattar R., Cairns B.R., and Marmorstein R. Structure and function of the SWIRM domain, a conserved protein module found in chromatin regulatory complexes. Proc Natl Acad Sci USA 103 (2006) 2057-2062
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2057-2062
    • Da, G.1    Lenkart, J.2    Zhao, K.3    Shiekhattar, R.4    Cairns, B.R.5    Marmorstein, R.6
  • 27
    • 0031874382 scopus 로고    scopus 로고
    • Formaldehyde cycle and the phases of stress syndrome
    • Tyihak E., Trezl L., and Szende B. Formaldehyde cycle and the phases of stress syndrome. Ann NY Acad Sci 851 (1998) 259-270
    • (1998) Ann NY Acad Sci , vol.851 , pp. 259-270
    • Tyihak, E.1    Trezl, L.2    Szende, B.3
  • 28
    • 33746435258 scopus 로고    scopus 로고
    • Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase
    • Yang M., Gocke C., Luo X., Borek D., Tomchick D., Machius M., Otwinowski Z., and Yu H. Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase. Mol Cell 23 (2006) 377-387
    • (2006) Mol Cell , vol.23 , pp. 377-387
    • Yang, M.1    Gocke, C.2    Luo, X.3    Borek, D.4    Tomchick, D.5    Machius, M.6    Otwinowski, Z.7    Yu, H.8
  • 29
    • 33845935787 scopus 로고    scopus 로고
    • A highly specific mechanism of histone H3-K4 recognition by histone demethylase LSD1
    • Forneris F., Binda C., Dall'Aglio A., Fraaije M.W., Battaglioli E., and Mattevi A. A highly specific mechanism of histone H3-K4 recognition by histone demethylase LSD1. J Biol Chem 281 (2006) 35289-35295
    • (2006) J Biol Chem , vol.281 , pp. 35289-35295
    • Forneris, F.1    Binda, C.2    Dall'Aglio, A.3    Fraaije, M.W.4    Battaglioli, E.5    Mattevi, A.6
  • 30
    • 0027936716 scopus 로고
    • Observation of two different chromophores in the resting state of monoamine oxidase B by fluorescence spectroscopy
    • Woo J.C.G., and Silverman R.B. Observation of two different chromophores in the resting state of monoamine oxidase B by fluorescence spectroscopy. Biochem Biophys Res Commun 202 (1994) 1574-1578
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 1574-1578
    • Woo, J.C.G.1    Silverman, R.B.2
  • 32
    • 0000897452 scopus 로고
    • A mechanism for mitochondrial monoamine oxidase catalyzed amine oxidation
    • Silverman R.B., Hoffman S.J., and Catus III W.B. A mechanism for mitochondrial monoamine oxidase catalyzed amine oxidation. J Am Chem Soc 102 (1980) 7126-7128
    • (1980) J Am Chem Soc , vol.102 , pp. 7126-7128
    • Silverman, R.B.1    Hoffman, S.J.2    Catus III, W.B.3
  • 33
    • 29244455626 scopus 로고    scopus 로고
    • Human histone demethylase LSD1 reads the histone code
    • This study describes the first detailed enzymatic study of a protein demethylase.
    • Forneris F., Binda C., Vanoni M.A., Battaglioli E., and Mattevi A. Human histone demethylase LSD1 reads the histone code. J Biol Chem 280 (2005) 41360-41365. This study describes the first detailed enzymatic study of a protein demethylase.
    • (2005) J Biol Chem , vol.280 , pp. 41360-41365
    • Forneris, F.1    Binda, C.2    Vanoni, M.A.3    Battaglioli, E.4    Mattevi, A.5
  • 34
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
    • Lee M.G., Wynder C., Cooch N., and Shiekhattar R. An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation. Nature 437 (2005) 432-435
    • (2005) Nature , vol.437 , pp. 432-435
    • Lee, M.G.1    Wynder, C.2    Cooch, N.3    Shiekhattar, R.4
  • 35
    • 24944535335 scopus 로고    scopus 로고
    • Regulation of LSD1 histone demethylase activity by its associated factors
    • Shi Y., Matson C., Lan F., Iwase S., Baba T., and Shi Y. Regulation of LSD1 histone demethylase activity by its associated factors. Mol Cell 19 (2005) 857-864
    • (2005) Mol Cell , vol.19 , pp. 857-864
    • Shi, Y.1    Matson, C.2    Lan, F.3    Iwase, S.4    Baba, T.5    Shi, Y.6
  • 38
    • 0021192474 scopus 로고
    • Suicide substrates, mechanism-based enzyme inactivators: recent developments
    • Walsh C.T. Suicide substrates, mechanism-based enzyme inactivators: recent developments. Annu Rev Biochem 53 (1984) 493-535
    • (1984) Annu Rev Biochem , vol.53 , pp. 493-535
    • Walsh, C.T.1
  • 39
    • 0028930481 scopus 로고
    • Mechanism-based enzyme inactivators
    • Silverman R.B. Mechanism-based enzyme inactivators. Methods Enzymol 249 (1995) 240-283
    • (1995) Methods Enzymol , vol.249 , pp. 240-283
    • Silverman, R.B.1
  • 40
    • 33646061354 scopus 로고    scopus 로고
    • A mechanism-based inactivator for histone demethylase LSD1
    • This paper is the first report of high potency inhibitors of LSD1.
    • Culhane J.C., Szewczuk L.M., Liu X., Da G., Marmorstein R., and Cole P.A. A mechanism-based inactivator for histone demethylase LSD1. J Am Chem Soc 128 (2006) 4536-4537. This paper is the first report of high potency inhibitors of LSD1.
    • (2006) J Am Chem Soc , vol.128 , pp. 4536-4537
    • Culhane, J.C.1    Szewczuk, L.M.2    Liu, X.3    Da, G.4    Marmorstein, R.5    Cole, P.A.6
  • 41
    • 34249881352 scopus 로고    scopus 로고
    • Structural basis for histone demethylation by LSD1 revealed by suicide inactivation
    • This paper reveals the first structural analysis of a histone demethylase in complex with its substrate with the surprising observation of gamma turns.
    • Yang M., Culhane J.C., Szewczuk L.M., Gocke C.B., Brautigam C.A., Tomchick D.R., Machius M., Cole P.A., and Yu H. Structural basis for histone demethylation by LSD1 revealed by suicide inactivation. Nat Struct Mol Biol 14 (2007) 535-539. This paper reveals the first structural analysis of a histone demethylase in complex with its substrate with the surprising observation of gamma turns.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 535-539
    • Yang, M.1    Culhane, J.C.2    Szewczuk, L.M.3    Gocke, C.B.4    Brautigam, C.A.5    Tomchick, D.R.6    Machius, M.7    Cole, P.A.8    Yu, H.9
  • 44
    • 33745187327 scopus 로고    scopus 로고
    • Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications
    • This paper is the first report that a clinically used monoamine oxidase inhibitor, despite its dissimilarity to a histone, can inhibit a histone demethylase.
    • Lee M.G., Wynder C., Schmidt D.M., McCafferty D.G., and Shiekhatter R. Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications. Chem Biol 13 (2006) 563-567. This paper is the first report that a clinically used monoamine oxidase inhibitor, despite its dissimilarity to a histone, can inhibit a histone demethylase.
    • (2006) Chem Biol , vol.13 , pp. 563-567
    • Lee, M.G.1    Wynder, C.2    Schmidt, D.M.3    McCafferty, D.G.4    Shiekhatter, R.5
  • 45
    • 34147173308 scopus 로고    scopus 로고
    • Trans-2-phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1
    • Schmidt D.M., and McCafferty D.G. Trans-2-phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1. Biochemistry 46 (2007) 4408-4416
    • (2007) Biochemistry , vol.46 , pp. 4408-4416
    • Schmidt, D.M.1    McCafferty, D.G.2
  • 46
    • 34447338875 scopus 로고    scopus 로고
    • Structural basis for inhibition of the LSD1 histone demethylase by the antidepressant trans-2-Phenylcyclopropylamine
    • Yang M., Culhane J.C., Szewczuk L.M., Jalili P., Ball H.L., Machius M., Cole P.A., and Yu H. Structural basis for inhibition of the LSD1 histone demethylase by the antidepressant trans-2-Phenylcyclopropylamine. Biochemistry 46 (2007) 8058-8065
    • (2007) Biochemistry , vol.46 , pp. 8058-8065
    • Yang, M.1    Culhane, J.C.2    Szewczuk, L.M.3    Jalili, P.4    Ball, H.L.5    Machius, M.6    Cole, P.A.7    Yu, H.8
  • 47
    • 34249934238 scopus 로고    scopus 로고
    • Inhibition of lysine-specific demethylase 1 by polyamine analogues results in reexpression of aberrantly silenced genes
    • Huang Y., Greene E., Stewart T.M., Goodwin A.C., Baylin P.M., and Casero Jr. R.A. Inhibition of lysine-specific demethylase 1 by polyamine analogues results in reexpression of aberrantly silenced genes. Proc Natl Acad Sci USA 104 (2007) 8023-8028
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8023-8028
    • Huang, Y.1    Greene, E.2    Stewart, T.M.3    Goodwin, A.C.4    Baylin, P.M.5    Casero Jr., R.A.6
  • 51
    • 34547132094 scopus 로고    scopus 로고
    • Structural basis of LSD1-CoREST selectivity in histone H3 recognition
    • Forneris F., Binda C., Adamo A., Battaglioli E., and Mattevi A. Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J Biol Chem 282 (2007) 20070-20074
    • (2007) J Biol Chem , vol.282 , pp. 20070-20074
    • Forneris, F.1    Binda, C.2    Adamo, A.3    Battaglioli, E.4    Mattevi, A.5


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