메뉴 건너뛰기




Volumn 20, Issue 6, 2010, Pages 739-748

Structural insights into histone lysine demethylation

Author keywords

[No Author keywords available]

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); FLAVINE ADENINE NUCLEOTIDE; HISTONE DEACETYLASE INHIBITOR; HISTONE H3; HISTONE LYSINE DEMETHYLASE 1; JUMONJI C TERMINAL DOMAIN PROTEIN; OXIDOREDUCTASE; PARGYLINE; PROTEIN KDM7A; PROTEIN PHF8; RECOMBINANT ENZYME; TRANYLCYPROMINE; UNCLASSIFIED DRUG;

EID: 78649664485     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2010.09.006     Document Type: Review
Times cited : (153)

References (53)
  • 1
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., Allis C.D. Translating the histone code. Science 2001, 293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 2
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin C., Zhang Y. The diverse functions of histone lysine methylation. Nat Rev Mol Cell Biol 2005, 6:838-849.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 3
    • 77953644347 scopus 로고    scopus 로고
    • Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases
    • Mosammaparast N., Shi Y. Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases. Annu Rev Biochem 2010, 79:155-179.
    • (2010) Annu Rev Biochem , vol.79 , pp. 155-179
    • Mosammaparast, N.1    Shi, Y.2
  • 6
    • 0035852637 scopus 로고    scopus 로고
    • CoREST is an integral component of the CoREST-human histone deacetylase complex
    • You A., Tong J.K., Grozinger C.M., Schreiber S.L. CoREST is an integral component of the CoREST-human histone deacetylase complex. Proc Natl Acad Sci USA 2001, 98:1454-1458.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1454-1458
    • You, A.1    Tong, J.K.2    Grozinger, C.M.3    Schreiber, S.L.4
  • 8
    • 0037470142 scopus 로고    scopus 로고
    • A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes
    • Hakimi M.A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R. A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes. J Biol Chem 2003, 278:7234-7239.
    • (2003) J Biol Chem , vol.278 , pp. 7234-7239
    • Hakimi, M.A.1    Dong, Y.2    Lane, W.S.3    Speicher, D.W.4    Shiekhattar, R.5
  • 9
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
    • Lee M.G., Wynder C., Cooch N., Shiekhattar R. An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation. Nature 2005, 437:432-435.
    • (2005) Nature , vol.437 , pp. 432-435
    • Lee, M.G.1    Wynder, C.2    Cooch, N.3    Shiekhattar, R.4
  • 10
    • 24944535335 scopus 로고    scopus 로고
    • Regulation of LSD1 histone demethylase activity by its associated factors
    • Shi Y.J., Matson C., Lan F., Iwase S., Baba T., Shi Y. Regulation of LSD1 histone demethylase activity by its associated factors. Mol Cell 2005, 19:857-864.
    • (2005) Mol Cell , vol.19 , pp. 857-864
    • Shi, Y.J.1    Matson, C.2    Lan, F.3    Iwase, S.4    Baba, T.5    Shi, Y.6
  • 13
    • 34547785073 scopus 로고    scopus 로고
    • Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1
    • Saleque S., Kim J., Rooke H.M., Orkin S.H. Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1. Mol Cell 2007, 27:562-572.
    • (2007) Mol Cell , vol.27 , pp. 562-572
    • Saleque, S.1    Kim, J.2    Rooke, H.M.3    Orkin, S.H.4
  • 14
    • 68749108259 scopus 로고    scopus 로고
    • LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer
    • Wang Y., Zhang H., Chen Y., Sun Y., Yang F., Yu W., Liang J., Sun L., Yang X., Shi L., et al. LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer. Cell 2009, 138:660-672.
    • (2009) Cell , vol.138 , pp. 660-672
    • Wang, Y.1    Zhang, H.2    Chen, Y.3    Sun, Y.4    Yang, F.5    Yu, W.6    Liang, J.7    Sun, L.8    Yang, X.9    Shi, L.10
  • 17
    • 33745862395 scopus 로고    scopus 로고
    • Crystal structure and mechanism of human lysine-specific demethylase-1
    • Stavropoulos P., Blobel G., Hoelz A. Crystal structure and mechanism of human lysine-specific demethylase-1. Nat Struct Mol Biol 2006, 13:626-632.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 626-632
    • Stavropoulos, P.1    Blobel, G.2    Hoelz, A.3
  • 18
    • 33746435258 scopus 로고    scopus 로고
    • Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase
    • Yang M., Gocke C.B., Luo X., Borek D., Tomchick D.R., Machius M., Otwinowski Z., Yu H. Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase. Mol Cell 2006, 23:377-387.
    • (2006) Mol Cell , vol.23 , pp. 377-387
    • Yang, M.1    Gocke, C.B.2    Luo, X.3    Borek, D.4    Tomchick, D.R.5    Machius, M.6    Otwinowski, Z.7    Yu, H.8
  • 20
    • 34548519907 scopus 로고    scopus 로고
    • A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase
    • Binda C., Coda A., Angelini R., Federico R., Ascenzi P., Mattevi A. A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase. Structure 1999, 7:265-276.
    • (1999) Structure , vol.7 , pp. 265-276
    • Binda, C.1    Coda, A.2    Angelini, R.3    Federico, R.4    Ascenzi, P.5    Mattevi, A.6
  • 23
  • 25
    • 34547132094 scopus 로고    scopus 로고
    • Structural basis of LSD1-CoREST selectivity in histone H3 recognition
    • Forneris F., Binda C., Adamo A., Battaglioli E., Mattevi A. Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J Biol Chem 2007, 282:20070-20074.
    • (2007) J Biol Chem , vol.282 , pp. 20070-20074
    • Forneris, F.1    Binda, C.2    Adamo, A.3    Battaglioli, E.4    Mattevi, A.5
  • 27
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden J.E., Peart M.J., Johnstone R.W. Anticancer activities of histone deacetylase inhibitors. Nat Rev Drug Discov 2006, 5:769-784.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 28
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S., Pelicci P.G. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 2006, 6:38-51.
    • (2006) Nat Rev Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 30
    • 33745187327 scopus 로고    scopus 로고
    • Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications
    • Lee M.G., Wynder C., Schmidt D.M., McCafferty D.G., Shiekhattar R. Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications. Chem Biol 2006, 13:563-567.
    • (2006) Chem Biol , vol.13 , pp. 563-567
    • Lee, M.G.1    Wynder, C.2    Schmidt, D.M.3    McCafferty, D.G.4    Shiekhattar, R.5
  • 31
    • 34447338875 scopus 로고    scopus 로고
    • Structural basis for the 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., Yu H. Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine. Biochemistry 2007, 46:8058-8065.
    • (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
  • 34
    • 77949421463 scopus 로고    scopus 로고
    • Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors
    • Culhane J.C., Wang D., Yen P.M., Cole P.A. Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors. J Am Chem Soc 2010, 132:3164-3176.
    • (2010) J Am Chem Soc , vol.132 , pp. 3164-3176
    • Culhane, J.C.1    Wang, D.2    Yen, P.M.3    Cole, P.A.4
  • 36
    • 77955025931 scopus 로고    scopus 로고
    • Structurally designed Trans-2-phenylcyclopropylamine derivatives potently inhibit histone demethylase LSD1/KDM1
    • Mimasu S., Umezawa N., Sato S., Higuchi T., Umehara T., Yokoyama S. Structurally designed Trans-2-phenylcyclopropylamine derivatives potently inhibit histone demethylase LSD1/KDM1. Biochemistry 2010, 49:6494-6503.
    • (2010) Biochemistry , vol.49 , pp. 6494-6503
    • Mimasu, S.1    Umezawa, N.2    Sato, S.3    Higuchi, T.4    Umehara, T.5    Yokoyama, S.6
  • 37
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • Klose R.J., Kallin E.M., Zhang Y. JmjC-domain-containing proteins and histone demethylation. Nat Rev Genet 2006, 7:715-727.
    • (2006) Nat Rev Genet , vol.7 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 43
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
    • Horton J.R., Upadhyay A.K., Qi H.H., Zhang X., Shi Y., Cheng X. Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. Nat Struct Mol Biol 2010, 17:38-43.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 38-43
    • Horton, J.R.1    Upadhyay, A.K.2    Qi, H.H.3    Zhang, X.4    Shi, Y.5    Cheng, X.6
  • 44
    • 77955267400 scopus 로고    scopus 로고
    • Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans
    • Yang Y., Hu L., Wang P., Hou H., Lin Y., Liu Y., Li Z., Gong R., Feng X., Zhou L., et al. Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans. Cell Res 2010, 20:886-898.
    • (2010) Cell Res , vol.20 , pp. 886-898
    • Yang, Y.1    Hu, L.2    Wang, P.3    Hou, H.4    Lin, Y.5    Liu, Y.6    Li, Z.7    Gong, R.8    Feng, X.9    Zhou, L.10
  • 46
    • 77955345001 scopus 로고    scopus 로고
    • Design, synthesis, enzyme-inhibitory activity, and effect on human cancer cells of a novel series of jumonji domain-containing protein 2 histone demethylase inhibitors
    • Hamada S., Suzuki T., Mino K., Koseki K., Oehme F., Flamme I., Ozasa H., Itoh Y., Ogasawara D., Komaarashi H., et al. Design, synthesis, enzyme-inhibitory activity, and effect on human cancer cells of a novel series of jumonji domain-containing protein 2 histone demethylase inhibitors. J Med Chem 2010, 53:5629-5638.
    • (2010) J Med Chem , vol.53 , pp. 5629-5638
    • Hamada, S.1    Suzuki, T.2    Mino, K.3    Koseki, K.4    Oehme, F.5    Flamme, I.6    Ozasa, H.7    Itoh, Y.8    Ogasawara, D.9    Komaarashi, H.10
  • 49
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • Jacobs S.A., Khorasanizadeh S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 2002, 295:2080-2083.
    • (2002) Science , vol.295 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 50
    • 77955273322 scopus 로고    scopus 로고
    • Coordinated regulation of active and repressive histone methylations by a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans
    • Lin H., Wang Y., Tian F., Pu P., Yu Y., Mao H., Yang Y., Wang P., Hu L., Lin Y., et al. Coordinated regulation of active and repressive histone methylations by a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans. Cell Res 2010, 20:899-907.
    • (2010) Cell Res , vol.20 , pp. 899-907
    • Lin, H.1    Wang, Y.2    Tian, F.3    Pu, P.4    Yu, Y.5    Mao, H.6    Yang, Y.7    Wang, P.8    Hu, L.9    Lin, Y.10
  • 51
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang Y., Fang J., Bedford M.T., Zhang Y., Xu R.M. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 2006, 312:748-751.
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 52
    • 37849015924 scopus 로고    scopus 로고
    • Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor
    • Lee J., Thompson J.R., Botuyan M.V., Mer G. Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Nat Struct Mol Biol 2008, 15:109-111.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 109-111
    • Lee, J.1    Thompson, J.R.2    Botuyan, M.V.3    Mer, G.4
  • 53
    • 44849100496 scopus 로고    scopus 로고
    • Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation
    • McGinty R.K., Kim J., Chatterjee C., Roeder R.G., Muir T.W. Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation. Nature 2008, 453:812-816.
    • (2008) Nature , vol.453 , pp. 812-816
    • McGinty, R.K.1    Kim, J.2    Chatterjee, C.3    Roeder, R.G.4    Muir, T.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.