메뉴 건너뛰기




Volumn 24, Issue 6, 2014, Pages 377-386

Mechanisms of functional promiscuity by HP1 proteins

Author keywords

Chromatin; Conformational flexibility; Functional versatility; HP1

Indexed keywords

HETEROCHROMATIN PROTEIN 1; HETEROCHROMATIN-SPECIFIC NONHISTONE CHROMOSOMAL PROTEIN HP-1; NONHISTONE PROTEIN; NUCLEOSOME;

EID: 84901470319     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2014.01.002     Document Type: Review
Times cited : (161)

References (97)
  • 1
    • 0036591876 scopus 로고    scopus 로고
    • Chromatin as a eukaryotic template of genetic information
    • Cavalli G. Chromatin as a eukaryotic template of genetic information. Curr. Opin. Cell Biol. 2002, 14:269-278.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 269-278
    • Cavalli, G.1
  • 2
    • 0035316574 scopus 로고    scopus 로고
    • Chromosome territories, nuclear architecture and gene regulation in mammalian cells
    • Cremer T., Cremer C. Chromosome territories, nuclear architecture and gene regulation in mammalian cells. Nat. Rev. Genet. 2001, 2:292-301.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 292-301
    • Cremer, T.1    Cremer, C.2
  • 3
    • 84951603510 scopus 로고
    • Beitraege zur Kenntniss der Zelle und ihrer Lebenserscheinungen
    • (in German)
    • Flemming W. Beitraege zur Kenntniss der Zelle und ihrer Lebenserscheinungen. Arch. Mikroskop. Anat. 1878, 16:302-436. (in German).
    • (1878) Arch. Mikroskop. Anat. , vol.16 , pp. 302-436
    • Flemming, W.1
  • 5
    • 0000251397 scopus 로고
    • Das Heterochromatin der Moose, 1
    • (in German)
    • Heitz E. Das Heterochromatin der Moose, 1. Jahrb. Wiss. Bot. 1928, 69:762-818. (in German).
    • (1928) Jahrb. Wiss. Bot. , vol.69 , pp. 762-818
    • Heitz, E.1
  • 6
    • 0000540894 scopus 로고
    • Heterochromatin, Chromocentren, Chromomeren
    • (in German)
    • Heitz E. Heterochromatin, Chromocentren, Chromomeren. Ber. Dtsch. Bot. Ges. 1929, 47:274-284. (in German).
    • (1929) Ber. Dtsch. Bot. Ges. , vol.47 , pp. 274-284
    • Heitz, E.1
  • 8
    • 0022818549 scopus 로고
    • Identification of a nonhistone chromosomal protein associated with heterochromatin in Drosophila melanogaster and its gene
    • James T., Elgin S. Identification of a nonhistone chromosomal protein associated with heterochromatin in Drosophila melanogaster and its gene. Mol. Cell. Biol. 1986, 6:3862-3872.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3862-3872
    • James, T.1    Elgin, S.2
  • 9
    • 0025600929 scopus 로고
    • Mutation in a heterochromatin-specific chromosomal protein is associated with suppression of position-effect variegation in Drosophila melanogaster
    • Eissenberg J.C., et al. Mutation in a heterochromatin-specific chromosomal protein is associated with suppression of position-effect variegation in Drosophila melanogaster. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:9923-9927.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 9923-9927
    • Eissenberg, J.C.1
  • 10
    • 48649098098 scopus 로고
    • The frequency of translocations produced by X-rays in Drosophila
    • Muller H.J., Altenburg E. The frequency of translocations produced by X-rays in Drosophila. Genetics 1930, 15:283-311.
    • (1930) Genetics , vol.15 , pp. 283-311
    • Muller, H.J.1    Altenburg, E.2
  • 11
    • 0014171555 scopus 로고
    • Single-locus modification of position-effect variegation in Drosophila melanogaster. I. White variegation
    • Spofford J.B. Single-locus modification of position-effect variegation in Drosophila melanogaster. I. White variegation. Genetics 1967, 57:751-766.
    • (1967) Genetics , vol.57 , pp. 751-766
    • Spofford, J.B.1
  • 12
    • 0026458066 scopus 로고
    • Heterochromatin protein 1, a known suppressor of position-effect variegation, is highly conserved in Drosophila
    • Clark R.F., Elgin S.C. Heterochromatin protein 1, a known suppressor of position-effect variegation, is highly conserved in Drosophila. Nucleic Acids Res. 1992, 20:6067-6074.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6067-6074
    • Clark, R.F.1    Elgin, S.C.2
  • 13
    • 0029645289 scopus 로고
    • Functional analysis of the chromo domain of HP1
    • Platero J.S., et al. Functional analysis of the chromo domain of HP1. EMBO J. 1995, 14:3977-3986.
    • (1995) EMBO J. , vol.14 , pp. 3977-3986
    • Platero, J.S.1
  • 14
    • 0032055402 scopus 로고    scopus 로고
    • Unfolding the mysteries of heterochromatin
    • Wallrath L.L. Unfolding the mysteries of heterochromatin. Curr. Opin. Genet. Dev. 1998, 8:147-153.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 147-153
    • Wallrath, L.L.1
  • 15
    • 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 2000, 406:593-599.
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1
  • 16
    • 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 2001, 410:120-124.
    • (2001) Nature , vol.410 , pp. 120-124
    • Bannister, A.J.1
  • 17
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M., et al. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 2001, 410:116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1
  • 18
    • 17944380227 scopus 로고    scopus 로고
    • Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability
    • Peters A.H.F.M., et al. Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability. Cell 2001, 107:323-337.
    • (2001) Cell , vol.107 , pp. 323-337
    • Peters, A.H.F.M.1
  • 19
    • 0034194376 scopus 로고    scopus 로고
    • Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis
    • Cowieson N.P., et al. Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis. Curr. Biol. 2000, 10:517-525.
    • (2000) Curr. Biol. , vol.10 , pp. 517-525
    • Cowieson, N.P.1
  • 20
    • 0033965983 scopus 로고    scopus 로고
    • The HP1 chromo shadow domain binds a consensus peptide pentamer
    • Smothers J.F., Henikoff S. The HP1 chromo shadow domain binds a consensus peptide pentamer. Curr. Biol. 2000, 10:27-30.
    • (2000) Curr. Biol. , vol.10 , pp. 27-30
    • Smothers, J.F.1    Henikoff, S.2
  • 21
    • 0036775704 scopus 로고    scopus 로고
    • Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1alpha
    • Muchardt C., et al. Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1alpha. EMBO Rep. 2002, 3:975-981.
    • (2002) EMBO Rep. , vol.3 , pp. 975-981
    • Muchardt, C.1
  • 22
    • 0038613861 scopus 로고    scopus 로고
    • HP1 binding to native chromatin in vitro is determined by the hinge region and not by the chromodomain
    • Meehan R.R., et al. HP1 binding to native chromatin in vitro is determined by the hinge region and not by the chromodomain. EMBO J. 2003, 22:3164-3174.
    • (2003) EMBO J. , vol.22 , pp. 3164-3174
    • Meehan, R.R.1
  • 23
    • 0037423688 scopus 로고    scopus 로고
    • Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1
    • Yamamoto K., Sonoda M. Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1. Biochem. Biophys. Res. Commun. 2003, 301:287-292.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 287-292
    • Yamamoto, K.1    Sonoda, M.2
  • 24
    • 0032960109 scopus 로고    scopus 로고
    • Functional domain structure of human heterochromatin protein HP1(Hsalpha): involvement of internal DNA-binding and C-terminal self-association domains in the formation of discrete dots in interphase nuclei
    • Yamada T., et al. Functional domain structure of human heterochromatin protein HP1(Hsalpha): involvement of internal DNA-binding and C-terminal self-association domains in the formation of discrete dots in interphase nuclei. J. Biochem. 1999, 125:832-837.
    • (1999) J. Biochem. , vol.125 , pp. 832-837
    • Yamada, T.1
  • 25
    • 23044431656 scopus 로고    scopus 로고
    • Histone H3 lysine 9 methylation and HP1gamma are associated with transcription elongation through mammalian chromatin
    • Vakoc C.R., et al. Histone H3 lysine 9 methylation and HP1gamma are associated with transcription elongation through mammalian chromatin. Mol. Cell 2005, 19:381-391.
    • (2005) Mol. Cell , vol.19 , pp. 381-391
    • Vakoc, C.R.1
  • 26
    • 40249085830 scopus 로고    scopus 로고
    • Regulation of an inducible promoter by an HP1beta-HP1gamma switch
    • Mateescu B., et al. Regulation of an inducible promoter by an HP1beta-HP1gamma switch. EMBO Rep. 2008, 9:267-272.
    • (2008) EMBO Rep. , vol.9 , pp. 267-272
    • Mateescu, B.1
  • 27
    • 79951899282 scopus 로고    scopus 로고
    • HP1c casts light on dark matter
    • Kwon S.H., Workman J.L. HP1c casts light on dark matter. Cell Cycle 2011, 10:625-630.
    • (2011) Cell Cycle , vol.10 , pp. 625-630
    • Kwon, S.H.1    Workman, J.L.2
  • 28
    • 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. Nat. Cell Biol. 2002, 4:89-93.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 89-93
    • Nonaka, N.1
  • 29
    • 51649110069 scopus 로고    scopus 로고
    • Heterochromatin links to centromeric protection by recruiting shugoshin
    • Yamagishi Y., et al. Heterochromatin links to centromeric protection by recruiting shugoshin. Nature 2008, 455:251-255.
    • (2008) Nature , vol.455 , pp. 251-255
    • Yamagishi, Y.1
  • 30
    • 0041384110 scopus 로고    scopus 로고
    • Cell cycle behavior of human HP1 subtypes: distinct molecular domains of HP1 are required for their centromeric localization during interphase and metaphase
    • Hayakawa T., et al. Cell cycle behavior of human HP1 subtypes: distinct molecular domains of HP1 are required for their centromeric localization during interphase and metaphase. J. Cell Sci. 2003, 116:3327-3338.
    • (2003) J. Cell Sci. , vol.116 , pp. 3327-3338
    • Hayakawa, T.1
  • 31
    • 3342926035 scopus 로고    scopus 로고
    • Human Orc2 localizes to centrosomes, centromeres and heterochromatin during chromosome inheritance
    • Prasanth S.G., et al. Human Orc2 localizes to centrosomes, centromeres and heterochromatin during chromosome inheritance. EMBO J. 2004, 23:2651-2663.
    • (2004) EMBO J. , vol.23 , pp. 2651-2663
    • Prasanth, S.G.1
  • 32
    • 4143116771 scopus 로고    scopus 로고
    • HP1 controls telomere capping, telomere elongation, and telomere silencing by two different mechanisms in Drosophila
    • Perrini B., et al. HP1 controls telomere capping, telomere elongation, and telomere silencing by two different mechanisms in Drosophila. Mol. Cell 2004, 15:467-476.
    • (2004) Mol. Cell , vol.15 , pp. 467-476
    • Perrini, B.1
  • 33
    • 80052468708 scopus 로고    scopus 로고
    • A role for heterochromatin protein 1γ at human telomeres
    • Canudas S., et al. A role for heterochromatin protein 1γ at human telomeres. Genes Dev. 2011, 25:1807-1819.
    • (2011) Genes Dev. , vol.25 , pp. 1807-1819
    • Canudas, S.1
  • 34
    • 71949105212 scopus 로고    scopus 로고
    • The emerging role of HP1 in the DNA damage response
    • Dinant C., Luijsterburg M.S. The emerging role of HP1 in the DNA damage response. Mol. Cell. Biol. 2009, 29:6335-6340.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 6335-6340
    • Dinant, C.1    Luijsterburg, M.S.2
  • 35
    • 66149094160 scopus 로고    scopus 로고
    • Heterochromatin protein 1 is recruited to various types of DNA damage
    • Luijsterburg M.S., et al. Heterochromatin protein 1 is recruited to various types of DNA damage. J. Cell Biol. 2009, 185:577-586.
    • (2009) J. Cell Biol. , vol.185 , pp. 577-586
    • Luijsterburg, M.S.1
  • 36
    • 84875517379 scopus 로고    scopus 로고
    • Differential contribution of HP1 proteins to DNA end resection and homology-directed repair
    • Soria G., Almouzni G. Differential contribution of HP1 proteins to DNA end resection and homology-directed repair. Cell Cycle 2013, 12:422-429.
    • (2013) Cell Cycle , vol.12 , pp. 422-429
    • Soria, G.1    Almouzni, G.2
  • 37
    • 60549110477 scopus 로고    scopus 로고
    • Chromatin binding of SRp20 and ASF/SF2 and dissociation from mitotic chromosomes is modulated by histone H3 serine 10 phosphorylation
    • Loomis R.J., et al. Chromatin binding of SRp20 and ASF/SF2 and dissociation from mitotic chromosomes is modulated by histone H3 serine 10 phosphorylation. Mol. Cell 2009, 33:450-461.
    • (2009) Mol. Cell , vol.33 , pp. 450-461
    • Loomis, R.J.1
  • 38
    • 79952364016 scopus 로고    scopus 로고
    • Histone H3 lysine 9 trimethylation and HP1γ favor inclusion of alternative exons
    • Saint-André V., et al. Histone H3 lysine 9 trimethylation and HP1γ favor inclusion of alternative exons. Nat. Struct. Mol. Biol. 2011, 18:337-344.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 337-344
    • Saint-André, V.1
  • 39
    • 78650961149 scopus 로고    scopus 로고
    • Epigenetics in alternative pre-mRNA splicing
    • Luco R.F., et al. Epigenetics in alternative pre-mRNA splicing. Cell 2011, 144:16-26.
    • (2011) Cell , vol.144 , pp. 16-26
    • Luco, R.F.1
  • 40
    • 84864048356 scopus 로고    scopus 로고
    • Phylogenomic analysis reveals dynamic evolutionary history of the Drosophila heterochromatin protein 1 (HP1) gene family
    • Levine M.T., et al. Phylogenomic analysis reveals dynamic evolutionary history of the Drosophila heterochromatin protein 1 (HP1) gene family. PLoS Genet. 2012, 8:e1002729.
    • (2012) PLoS Genet. , vol.8
    • Levine, M.T.1
  • 41
    • 73349091841 scopus 로고    scopus 로고
    • Multiple roles for heterochromatin protein 1 genes in Drosophila
    • Vermaak D., Malik H.S. Multiple roles for heterochromatin protein 1 genes in Drosophila. Annu. Rev. Genet. 2009, 43:467-492.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 467-492
    • Vermaak, D.1    Malik, H.S.2
  • 42
    • 84864618472 scopus 로고    scopus 로고
    • CBX3 regulates efficient RNA processing genome-wide
    • Smallwood A., et al. CBX3 regulates efficient RNA processing genome-wide. Genome Res. 2012, 22:1426-1436.
    • (2012) Genome Res. , vol.22 , pp. 1426-1436
    • Smallwood, A.1
  • 43
    • 75949121454 scopus 로고    scopus 로고
    • The essential function of HP1 beta: a case of the tail wagging the dog?
    • Billur M., et al. The essential function of HP1 beta: a case of the tail wagging the dog?. Trends Biochem. Sci. 2010, 35:115-123.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 115-123
    • Billur, M.1
  • 44
    • 77957662160 scopus 로고    scopus 로고
    • Heterochromatin protein 1 (HP1) connects the FACT histone chaperone complex to the phosphorylated CTD of RNA polymerase II
    • Kwon S.H., et al. Heterochromatin protein 1 (HP1) connects the FACT histone chaperone complex to the phosphorylated CTD of RNA polymerase II. Genes Dev. 2010, 24:2133-2145.
    • (2010) Genes Dev. , vol.24 , pp. 2133-2145
    • Kwon, S.H.1
  • 45
    • 0035102746 scopus 로고    scopus 로고
    • The hinge and chromo shadow domain impart distinct targeting of HP1-like proteins
    • Smothers J.F., Henikoff S. The hinge and chromo shadow domain impart distinct targeting of HP1-like proteins. Mol. Cell. Biol. 2001, 21:2555-2569.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2555-2569
    • Smothers, J.F.1    Henikoff, S.2
  • 46
    • 34748875248 scopus 로고    scopus 로고
    • Functional domain analysis of human HP1 isoforms in Drosophila
    • Kato M., et al. Functional domain analysis of human HP1 isoforms in Drosophila. Cell Struct. Funct. 2007, 32:57-67.
    • (2007) Cell Struct. Funct. , vol.32 , pp. 57-67
    • Kato, M.1
  • 47
    • 57349135362 scopus 로고    scopus 로고
    • Balance between distinct HP1 family proteins controls heterochromatin assembly in fission yeast
    • Sadaie M., et al. Balance between distinct HP1 family proteins controls heterochromatin assembly in fission yeast. Mol. Cell. Biol. 2008, 28:6973-6988.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6973-6988
    • Sadaie, M.1
  • 48
    • 79955068697 scopus 로고    scopus 로고
    • The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners
    • Mendez D.L., et al. The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners. Chembiochem 2011, 12:1084-1096.
    • (2011) Chembiochem , vol.12 , pp. 1084-1096
    • Mendez, D.L.1
  • 49
    • 84881223953 scopus 로고    scopus 로고
    • Heterochromatin protein 1a (HP1a) partner specificity is determined by critical amino acids in the chromo shadow domain and C-terminal extension
    • Mendez D.L., et al. Heterochromatin protein 1a (HP1a) partner specificity is determined by critical amino acids in the chromo shadow domain and C-terminal extension. J. Biol. Chem. 2013, 228:22315-22323.
    • (2013) J. Biol. Chem. , vol.228 , pp. 22315-22323
    • Mendez, D.L.1
  • 50
    • 33845192953 scopus 로고    scopus 로고
    • The heterochromatin protein 1 family
    • Lomberk G., et al. The heterochromatin protein 1 family. Genome Biol. 2006, 7:228.
    • (2006) Genome Biol. , vol.7 , pp. 228
    • Lomberk, G.1
  • 51
    • 44349122537 scopus 로고    scopus 로고
    • HP1: a functionally multifaceted protein
    • Fanti L., Pimpinelli S. HP1: a functionally multifaceted protein. Curr. Opin. Genet. Dev. 2008, 18:169-174.
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , pp. 169-174
    • Fanti, L.1    Pimpinelli, S.2
  • 52
    • 77949874234 scopus 로고    scopus 로고
    • Histone variants - ancient wrap artists of the epigenome
    • Talbert P.B., Henikoff S. Histone variants - ancient wrap artists of the epigenome. Nat. Rev. Mol. Cell Biol. 2010, 11:264-275.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 264-275
    • Talbert, P.B.1    Henikoff, S.2
  • 53
    • 0348150714 scopus 로고    scopus 로고
    • Maintenance of stable heterochromatin domains by dynamic HP1 binding
    • Cheutin T., et al. Maintenance of stable heterochromatin domains by dynamic HP1 binding. Science 2003, 299:721-725.
    • (2003) Science , vol.299 , pp. 721-725
    • Cheutin, T.1
  • 54
    • 2542497773 scopus 로고    scopus 로고
    • High- and low-mobility populations of HP1 in heterochromatin of mammalian cells
    • Schmiedeberg L., et al. High- and low-mobility populations of HP1 in heterochromatin of mammalian cells. Mol. Biol. Cell 2004, 15:2819-2833.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2819-2833
    • Schmiedeberg, L.1
  • 55
    • 72249109008 scopus 로고    scopus 로고
    • Multiscale analysis of dynamics and interactions of heterochromatin protein 1 by fluorescence fluctuation microscopy
    • Müller K.P., et al. Multiscale analysis of dynamics and interactions of heterochromatin protein 1 by fluorescence fluctuation microscopy. Biophys. J. 2009, 97:2876-2885.
    • (2009) Biophys. J. , vol.97 , pp. 2876-2885
    • Müller, K.P.1
  • 56
    • 1842505448 scopus 로고    scopus 로고
    • In vivo dynamics of Swi6 in yeast: evidence for a stochastic model of heterochromatin
    • Cheutin T., et al. In vivo dynamics of Swi6 in yeast: evidence for a stochastic model of heterochromatin. Mol. Cell. Biol. 2004, 24:3157-3167.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3157-3167
    • Cheutin, T.1
  • 57
    • 26944434789 scopus 로고    scopus 로고
    • The nucleation and maintenance of heterochromatin by a histone deacetylase in fission yeast
    • Yamada T., et al. The nucleation and maintenance of heterochromatin by a histone deacetylase in fission yeast. Mol. Cell 2005, 20:173-185.
    • (2005) Mol. Cell , vol.20 , pp. 173-185
    • Yamada, T.1
  • 58
    • 33846703987 scopus 로고    scopus 로고
    • SHREC, an effector complex for heterochromatic transcriptional silencing
    • Sugiyama T., et al. SHREC, an effector complex for heterochromatic transcriptional silencing. Cell 2007, 128:491-504.
    • (2007) Cell , vol.128 , pp. 491-504
    • Sugiyama, T.1
  • 59
    • 79953171493 scopus 로고    scopus 로고
    • Role of Swi6/HP1 self-association-mediated recruitment of Clr4/Suv39 in establishment and maintenance of heterochromatin in fission yeast
    • Haldar S., et al. Role of Swi6/HP1 self-association-mediated recruitment of Clr4/Suv39 in establishment and maintenance of heterochromatin in fission yeast. J. Biol. Chem. 2011, 286:9308-9320.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9308-9320
    • Haldar, S.1
  • 60
    • 84864315587 scopus 로고    scopus 로고
    • HP1(Swi6) mediates the recognition and destruction of heterochromatic RNA transcripts
    • Keller C., et al. HP1(Swi6) mediates the recognition and destruction of heterochromatic RNA transcripts. Mol. Cell 2012, 47:215-227.
    • (2012) Mol. Cell , vol.47 , pp. 215-227
    • Keller, C.1
  • 61
    • 47349112662 scopus 로고    scopus 로고
    • SiRNA-mediated heterochromatin establishment requires HP1 and is associated with antisense transcription
    • Iida T., et al. siRNA-mediated heterochromatin establishment requires HP1 and is associated with antisense transcription. Mol. Cell 2008, 31:178-189.
    • (2008) Mol. Cell , vol.31 , pp. 178-189
    • Iida, T.1
  • 62
    • 33744552663 scopus 로고    scopus 로고
    • Swi6/HP1 recruits a JmjC domain protein to facilitate transcription of heterochromatic repeats
    • Zofall M., Grewal S.I.S. Swi6/HP1 recruits a JmjC domain protein to facilitate transcription of heterochromatic repeats. Mol. Cell 2006, 22:681-692.
    • (2006) Mol. Cell , vol.22 , pp. 681-692
    • Zofall, M.1    Grewal, S.I.S.2
  • 63
    • 78650964584 scopus 로고    scopus 로고
    • 2 ubiquitin ligase inhibits invasion of a boundary-associated antisilencing factor into heterochromatin
    • 2 ubiquitin ligase inhibits invasion of a boundary-associated antisilencing factor into heterochromatin. Cell 2011, 144:41-54.
    • (2011) Cell , vol.144 , pp. 41-54
    • Braun, S.1
  • 64
    • 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 2002, 416:103-107.
    • (2002) Nature , vol.416 , pp. 103-107
    • Nielsen, P.R.1
  • 65
    • 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
  • 66
    • 79952259222 scopus 로고    scopus 로고
    • N-terminal phosphorylation of HP1{alpha} promotes its chromatin binding
    • Hiragami-Hamada K., et al. N-terminal phosphorylation of HP1{alpha} promotes its chromatin binding. Mol. Cell. Biol. 2011, 31:1186-1200.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1186-1200
    • Hiragami-Hamada, K.1
  • 67
    • 77955884904 scopus 로고    scopus 로고
    • Isoform-specific determinants in the HP1 binding to histone 3: insights from molecular simulations
    • Machado M.R., et al. Isoform-specific determinants in the HP1 binding to histone 3: insights from molecular simulations. Amino Acids 2010, 38:1571-1581.
    • (2010) Amino Acids , vol.38 , pp. 1571-1581
    • Machado, M.R.1
  • 68
    • 84876285368 scopus 로고    scopus 로고
    • A conformational switch in HP1 releases auto-inhibition to drive heterochromatin assembly
    • Canzio D., et al. A conformational switch in HP1 releases auto-inhibition to drive heterochromatin assembly. Nature 2013, 496:377-381.
    • (2013) Nature , vol.496 , pp. 377-381
    • Canzio, D.1
  • 69
    • 0033591234 scopus 로고    scopus 로고
    • Phosphorylation of heterochromatin protein 1 by casein kinase II is required for efficient heterochromatin binding in Drosophila
    • Zhao T., Eissenberg J.C. Phosphorylation of heterochromatin protein 1 by casein kinase II is required for efficient heterochromatin binding in Drosophila. J. Biol. Chem. 1999, 274:15095-15100.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15095-15100
    • Zhao, T.1    Eissenberg, J.C.2
  • 70
    • 0035937710 scopus 로고    scopus 로고
    • Phosphorylation site mutations in heterochromatin protein 1 (HP1) reduce or eliminate silencing activity
    • Zhao T., et al. Phosphorylation site mutations in heterochromatin protein 1 (HP1) reduce or eliminate silencing activity. J. Biol. Chem. 2001, 276:9512-9518.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9512-9518
    • Zhao, T.1
  • 71
    • 0033811254 scopus 로고    scopus 로고
    • Conservation of heterochromatin protein 1 function
    • Wang G., et al. Conservation of heterochromatin protein 1 function. Mol. Cell. Biol. 2000, 20:6970-6983.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6970-6983
    • Wang, G.1
  • 72
    • 78650734995 scopus 로고    scopus 로고
    • Chromodomain-mediated oligomerization of HP1 suggests a nucleosome-bridging mechanism for heterochromatin assembly
    • Canzio D., et al. Chromodomain-mediated oligomerization of HP1 suggests a nucleosome-bridging mechanism for heterochromatin assembly. Mol. Cell 2011, 41:67-81.
    • (2011) Mol. Cell , vol.41 , pp. 67-81
    • Canzio, D.1
  • 73
    • 72149127696 scopus 로고    scopus 로고
    • Heterochromatin protein 1 is extensively decorated with histone code-like post-translational modifications
    • LeRoy G., et al. Heterochromatin protein 1 is extensively decorated with histone code-like post-translational modifications. Mol. Cell. Proteomics 2009, 8:2432-2442.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2432-2442
    • LeRoy, G.1
  • 74
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by polycomb and HP1 chromodomains
    • Fischle W., et al. Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by polycomb and HP1 chromodomains. Genes Dev. 2003, 17:1870-1881.
    • (2003) Genes Dev. , vol.17 , pp. 1870-1881
    • Fischle, W.1
  • 75
    • 0035102746 scopus 로고    scopus 로고
    • The hinge and chromo shadow domain impart distinct targeting of HP1-like proteins
    • Smothers J., Henikoff S. The hinge and chromo shadow domain impart distinct targeting of HP1-like proteins. Mol. Cell. Biol. 2001, 21:2555-2569.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2555-2569
    • Smothers, J.1    Henikoff, S.2
  • 76
    • 70349975711 scopus 로고    scopus 로고
    • JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin
    • Dawson M.A., et al. JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin. Nature 2009, 461:819-822.
    • (2009) Nature , vol.461 , pp. 819-822
    • Dawson, M.A.1
  • 77
    • 74249112844 scopus 로고    scopus 로고
    • Interaction of HP1 and Brg1/Brm with the globular domain of histone H3 is required for HP1-mediated repression
    • Lavigne M., et al. Interaction of HP1 and Brg1/Brm with the globular domain of histone H3 is required for HP1-mediated repression. PLoS Genet. 2009, 5:e1000769.
    • (2009) PLoS Genet. , vol.5
    • Lavigne, M.1
  • 78
    • 84861557082 scopus 로고    scopus 로고
    • Characterization of the chromoshadow domain-mediated binding of heterochromatin protein 1 α (HP1α) to histone H3
    • Richart A.N., et al. Characterization of the chromoshadow domain-mediated binding of heterochromatin protein 1 α (HP1α) to histone H3. J. Biol. Chem. 2012, 287:18730-18737.
    • (2012) J. Biol. Chem. , vol.287 , pp. 18730-18737
    • Richart, A.N.1
  • 79
    • 0034599522 scopus 로고    scopus 로고
    • The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer
    • Brasher S.V., et al. The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer. EMBO J. 2000, 19:1587-1597.
    • (2000) EMBO J. , vol.19 , pp. 1587-1597
    • Brasher, S.V.1
  • 80
    • 10744228652 scopus 로고    scopus 로고
    • Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin
    • Thiru A., et al. Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin. EMBO J. 2004, 23:489-499.
    • (2004) EMBO J. , vol.23 , pp. 489-499
    • Thiru, A.1
  • 81
    • 79952189085 scopus 로고    scopus 로고
    • SUMOylation promotes de novo targeting of HP1α to pericentric heterochromatin
    • Maison C., et al. SUMOylation promotes de novo targeting of HP1α to pericentric heterochromatin. Nat. Genet. 2011, 43:220-227.
    • (2011) Nat. Genet. , vol.43 , pp. 220-227
    • Maison, C.1
  • 82
    • 58149513466 scopus 로고    scopus 로고
    • Phosphorylation of Swi6/HP1 regulates transcriptional gene silencing at heterochromatin
    • Shimada A., et al. Phosphorylation of Swi6/HP1 regulates transcriptional gene silencing at heterochromatin. Genes Dev. 2009, 23:18-23.
    • (2009) Genes Dev. , vol.23 , pp. 18-23
    • Shimada, A.1
  • 83
    • 13844280986 scopus 로고    scopus 로고
    • Mutations in the heterochromatin protein 1 (HP1) hinge domain affect HP1 protein interactions and chromosomal distribution
    • Badugu R., et al. Mutations in the heterochromatin protein 1 (HP1) hinge domain affect HP1 protein interactions and chromosomal distribution. Chromosoma 2005, 113:370-384.
    • (2005) Chromosoma , vol.113 , pp. 370-384
    • Badugu, R.1
  • 84
    • 0036787922 scopus 로고    scopus 로고
    • Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation
    • Zhang C.L., et al. Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation. Mol. Cell. Biol. 2002, 22:7302-7312.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7302-7312
    • Zhang, C.L.1
  • 85
    • 0032576619 scopus 로고    scopus 로고
    • INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1
    • Ainsztein A.M., et al. INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1. J. Cell Biol. 1998, 143:1763-1774.
    • (1998) J. Cell Biol. , vol.143 , pp. 1763-1774
    • Ainsztein, A.M.1
  • 86
    • 0141706646 scopus 로고    scopus 로고
    • Novel Drosophila heterochromatin protein 1 (HP1)/origin recognition complex-associated protein (HOAP) repeat motif in HP1/HOAP interactions and chromocenter associations
    • Badugu R., et al. Novel Drosophila heterochromatin protein 1 (HP1)/origin recognition complex-associated protein (HOAP) repeat motif in HP1/HOAP interactions and chromocenter associations. J. Biol. Chem. 2003, 278:34491-34498.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34491-34498
    • Badugu, R.1
  • 87
    • 33645725188 scopus 로고    scopus 로고
    • Evidence for the existence of an HP1-mediated subcode within the histone code
    • Lomberk G., et al. Evidence for the existence of an HP1-mediated subcode within the histone code. Nat. Cell Biol. 2006, 8:407-415.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 407-415
    • Lomberk, G.1
  • 88
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution - a 60-year-old hypothesis revisited
    • James L.C., Tawfik D.S. Conformational diversity and protein evolution - a 60-year-old hypothesis revisited. Trends Biochem. Sci. 2003, 28:361-368.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 89
    • 33748525883 scopus 로고    scopus 로고
    • Enzyme promiscuity: evolutionary and mechanistic aspects
    • Khersonsky O., et al. Enzyme promiscuity: evolutionary and mechanistic aspects. Curr. Opin. Chem. Biol. 2006, 10:498-508.
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 498-508
    • Khersonsky, O.1
  • 90
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • Tokuriki N., Tawfik D.S. Protein dynamism and evolvability. Science 2009, 324:203-207.
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 91
    • 80052340812 scopus 로고    scopus 로고
    • The role of protein conformational fluctuations in allostery, function, and evolution
    • Wrabl J.O., et al. The role of protein conformational fluctuations in allostery, function, and evolution. Biophys. Chem. 2011, 159:129-141.
    • (2011) Biophys. Chem. , vol.159 , pp. 129-141
    • Wrabl, J.O.1
  • 92
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: hubs for controlling the flow of cellular information
    • Good M.C., et al. Scaffold proteins: hubs for controlling the flow of cellular information. Science 2011, 332:680-686.
    • (2011) Science , vol.332 , pp. 680-686
    • Good, M.C.1
  • 93
    • 84879327823 scopus 로고    scopus 로고
    • Modulation of allostery by protein intrinsic disorder
    • Ferreon A.C., et al. Modulation of allostery by protein intrinsic disorder. Nature 2013, 498:390-394.
    • (2013) Nature , vol.498 , pp. 390-394
    • Ferreon, A.C.1
  • 94
    • 84876016764 scopus 로고    scopus 로고
    • Structural plasticity in human heterochromatin protein 1β
    • Munari F., et al. Structural plasticity in human heterochromatin protein 1β. PLoS ONE 2013, 8:e60887.
    • (2013) PLoS ONE , vol.8
    • Munari, F.1
  • 95
    • 84871808185 scopus 로고    scopus 로고
    • Hinge and chromoshadow of HP1α participate in recognition of K9 methylated histone H3 in nucleosomes
    • Mishima Y., et al. Hinge and chromoshadow of HP1α participate in recognition of K9 methylated histone H3 in nucleosomes. J. Mol. Biol. 2012, 425:54-70.
    • (2012) J. Mol. Biol. , vol.425 , pp. 54-70
    • Mishima, Y.1
  • 96
    • 84866924932 scopus 로고    scopus 로고
    • Methylation of lysine 9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1β with the nucleosome
    • Munari F., et al. Methylation of lysine 9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1β with the nucleosome. J. Biol. Chem. 2012, 287:33756-33765.
    • (2012) J. Biol. Chem. , vol.287 , pp. 33756-33765
    • Munari, F.1
  • 97
    • 0035019466 scopus 로고    scopus 로고
    • Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins
    • Nielsen A.L., et al. Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins. Mol. Cell 2001, 7:729-739.
    • (2001) Mol. Cell , vol.7 , pp. 729-739
    • Nielsen, A.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.