메뉴 건너뛰기




Volumn 438, Issue 7071, 2005, Pages 1176-1180

Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BIOTECHNOLOGY; CHEMICAL MODIFICATION;

EID: 28844475262     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature04254     Document Type: Article
Times cited : (551)

References (30)
  • 1
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. & Allis, C. D. Translating the histone code. Science 293, 1074-1080 (2001).
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 2
    • 0035282458 scopus 로고    scopus 로고
    • Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
    • Bannister, A. J. et al. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 410, 120-124 (2001).
    • (2001) Nature , vol.410 , pp. 120-124
    • Bannister, A.J.1
  • 3
    • 0035903443 scopus 로고    scopus 로고
    • Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3
    • Jacobs, S. A. et al. Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3. EMBO J. 20, 5232-5241 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5232-5241
    • Jacobs, S.A.1
  • 4
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner, M., O'Carroll, D., Rea, S., Mechtler, K. & Jenuwein, T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410, 116-120 (2001).
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 5
    • 0037034911 scopus 로고    scopus 로고
    • Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9
    • Nielsen, P. R. et al. Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. Nature 416, 103-107 (2002).
    • (2002) Nature , vol.416 , pp. 103-107
    • Nielsen, P.R.1
  • 6
    • 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 295, 2080-2083 (2002).
    • (2002) Science , vol.295 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 7
    • 0034604354 scopus 로고    scopus 로고
    • Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes
    • Hsu, J. Y. et al. Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell 102, 279-291 (2000).
    • (2000) Cell , vol.102 , pp. 279-291
    • Hsu, J.Y.1
  • 8
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle, W., Wang, Y. & Allis, C. D. Binary switches and modification cassettes in histone biology and beyond. Nature 425, 475-479 (2003).
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 9
    • 0033793915 scopus 로고    scopus 로고
    • Novel human autoantibodies to phosphoepitopes on mitotic chromosomal autoantigens (MCAs)
    • Gitlits, V. M., Macaulay, S. L., Toh, B. H. & Sentry, J. W. Novel human autoantibodies to phosphoepitopes on mitotic chromosomal autoantigens (MCAs). J. Investig. Med. 48, 172-182 (2000).
    • (2000) J. Investig. Med. , vol.48 , pp. 172-182
    • Gitlits, V.M.1    Macaulay, S.L.2    Toh, B.H.3    Sentry, J.W.4
  • 10
    • 0033212963 scopus 로고    scopus 로고
    • Heterochromatin dynamics in mouse cells: Interaction between chromatin assembly factor 1 and HP1 proteins
    • Murzina, N., Verreault, A., Laue, E. & Stillman, B. Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins. Mol. Cell 4, 529-540 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 529-540
    • Murzina, N.1    Verreault, A.2    Laue, E.3    Stillman, B.4
  • 11
    • 0035735597 scopus 로고    scopus 로고
    • Molecular behaviour in living mitotic cells of human centromere heterochromatin protein HPLα ectopically expressed as a fusion to red fluorescent protein
    • Sugimoto, K., Tasaka, H. & Dotsu, M. Molecular behaviour in living mitotic cells of human centromere heterochromatin protein HPLα ectopically expressed as a fusion to red fluorescent protein. Cell Struct. Funct. 26, 705-718 (2001).
    • (2001) Cell Struct. Funct. , vol.26 , pp. 705-718
    • Sugimoto, K.1    Tasaka, H.2    Dotsu, M.3
  • 13
    • 0035432975 scopus 로고    scopus 로고
    • Determining centromere identity: Cyclical stories and forking paths
    • Sullivan, B. A., Blower, M. D. & Karpen, G. H. Determining centromere identity: cyclical stories and forking paths. Nature Rev. Genet. 2, 584-596 (2001).
    • (2001) Nature Rev. Genet. , vol.2 , pp. 584-596
    • Sullivan, B.A.1    Blower, M.D.2    Karpen, G.H.3
  • 14
    • 0037380151 scopus 로고    scopus 로고
    • Stretching it: Putting the CEN(P-A) in centromere
    • Mellone, B. G. & Allshire, R. C. Stretching it: putting the CEN(P-A) in centromere. Curr. Opin. Genet. Dev. 13, 191-198 (2003).
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 191-198
    • Mellone, B.G.1    Allshire, R.C.2
  • 15
    • 3042794631 scopus 로고    scopus 로고
    • Building the centromere: From foundation proteins to 3D organization
    • Amor, D. J., Kalitsis, P., Sumer, H. & Choo, K. H. Building the centromere: from foundation proteins to 3D organization. Trends Cell Biol. 14, 359-368 (2004).
    • (2004) Trends Cell Biol. , vol.14 , pp. 359-368
    • Amor, D.J.1    Kalitsis, P.2    Sumer, H.3    Choo, K.H.4
  • 16
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyllysine marks in histone H3 by Polycomb and HP1 chromodomains
    • Fischle, W. et al. Molecular basis for the discrimination of repressive methyllysine marks in histone H3 by Polycomb and HP1 chromodomains. Genes Dev. 17, 1870-1881 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 1870-1881
    • Fischle, W.1
  • 17
    • 0035930750 scopus 로고    scopus 로고
    • Requirement of heterochromatin for cohesion at centromeres
    • Bernard, P. et al. Requirement of heterochromatin for cohesion at centromeres. Science 294, 2539-2542 (2001).
    • (2001) Science , vol.294 , pp. 2539-2542
    • Bernard, P.1
  • 18
    • 0036144420 scopus 로고    scopus 로고
    • Recruitment of cohesin to heterochromatic regions by Swi6/HP1 in fission yeast
    • Nonaka, N. et al. Recruitment of cohesin to heterochromatic regions by Swi6/HP1 in fission yeast. Nature Cell Biol. 4, 89-93 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 89-93
    • Nonaka, N.1
  • 19
    • 2342517250 scopus 로고    scopus 로고
    • Regulation of heterochromatin by histone methylation and small RNAs
    • Grewal, S. I. & Rice, J. C. Regulation of heterochromatin by histone methylation and small RNAs. Curr. Opin. Cell Biol. 16, 230-238 (2004).
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 230-238
    • Grewal, S.I.1    Rice, J.C.2
  • 20
    • 0022552491 scopus 로고
    • Three human chromosomal autoantigens are recognized by sera from patients with anticentromere antibodies
    • Earnshaw, W., Bordwell, B., Marino, C. & Rothfield, N. Three human chromosomal autoantigens are recognized by sera from patients with anticentromere antibodies. J. Clin. Invest. 77, 426-430 (1986).
    • (1986) J. Clin. Invest. , vol.77 , pp. 426-430
    • Earnshaw, W.1    Bordwell, B.2    Marino, C.3    Rothfield, N.4
  • 21
    • 0038746733 scopus 로고    scopus 로고
    • The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint
    • Hauf, S. et al. The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint. J. Cell Biol. 161, 281-294 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 281-294
    • Hauf, S.1
  • 22
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea, S. et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406, 593-599 (2000).
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1
  • 23
    • 0035911159 scopus 로고    scopus 로고
    • Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis
    • Giet, R. & Glover, D. M. Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis. J. Cell Biol. 152, 669-682 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 669-682
    • Giet, R.1    Glover, D.M.2
  • 24
    • 0142136096 scopus 로고    scopus 로고
    • Centromere silencing and function in fission yeast is governed by the amino terminus of histone H3
    • Mellone, B. G. et al. Centromere silencing and function in fission yeast is governed by the amino terminus of histone H3. Curr. Biol. 13, 1748-1757 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1748-1757
    • Mellone, B.G.1
  • 25
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • Wei, Y., Yu, L., Bowen, J., Gorovsky, M. A. & Allis, C. D. Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell 97, 99-109 (1999).
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3    Gorovsky, M.A.4    Allis, C.D.5
  • 26
    • 2942610993 scopus 로고    scopus 로고
    • Tethering of HP1 proteins to chromatin is relieved by phosphoacetylation of histone H3
    • Mateescu, B., England, P., Halgand, F., Yaniv, M. & Muchardt, C. Tethering of HP1 proteins to chromatin is relieved by phosphoacetylation of histone H3. EMBO Rep. 5, 490-496 (2004).
    • (2004) EMBO Rep. , vol.5 , pp. 490-496
    • Mateescu, B.1    England, P.2    Halgand, F.3    Yaniv, M.4    Muchardt, C.5
  • 27
    • 0036158780 scopus 로고    scopus 로고
    • Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation
    • Goto, H., Yasui, Y., Nigg, E. A. & Inagaki, M. Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation. Genes Cells 7, 11-17 (2002).
    • (2002) Genes Cells , vol.7 , pp. 11-17
    • Goto, H.1    Yasui, Y.2    Nigg, E.A.3    Inagaki, M.4
  • 28
    • 3142562589 scopus 로고    scopus 로고
    • Regulation of sister chromatid cohesion between chromosome arms
    • Gimenez-Abian, J. F. et al. Regulation of sister chromatid cohesion between chromosome arms. Curr. Biol. 14, 1187-1193 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 1187-1193
    • Gimenez-Abian, J.F.1
  • 29
    • 13444302537 scopus 로고    scopus 로고
    • Distinct functions of condensin I and II in mitotic chromosome assembly
    • Hirota, T., Gerlich, D., Koch, B., Ellenberg, J. & Peters, J. M. Distinct functions of condensin I and II in mitotic chromosome assembly. J. Cell Sci. 117, 6435-6445 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 6435-6445
    • Hirota, T.1    Gerlich, D.2    Koch, B.3    Ellenberg, J.4    Peters, J.M.5
  • 30
    • 20844436307 scopus 로고    scopus 로고
    • Mechanism of Aurora B activation by INCENP and inhibition by hesperadin
    • Sessa, F. et al. Mechanism of Aurora B activation by INCENP and inhibition by hesperadin. Mol. Cell 18, 379-391 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 379-391
    • Sessa, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.