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Volumn 10, Issue 1, 2015, Pages 138-145

Analysis of phosphorylation-dependent protein-protein interactions of histone H3

Author keywords

[No Author keywords available]

Indexed keywords

DEXTRO AMINO ACID; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE 1; HISTONE H3; PHOSPHONOMETHYLENALANINE; PROTEIN 14 3 3; RETINOBLASTOMA BINDING PROTEIN 7; SERINE; UNCLASSIFIED DRUG; AMINO ACID; HISTONE; HISTONE ACETYLTRANSFERASE TYPE B COMPLEX; ISOPROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 84921340616     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500563n     Document Type: Article
Times cited : (19)

References (49)
  • 2
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. and Allis, C. D. (2001) Translating the histone code Science 293, 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 3
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007) Chromatin modifications and their function Cell 128, 693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 4
    • 34548312353 scopus 로고    scopus 로고
    • Histone proteomics and the epigenetic regulation of nucleosome mobility
    • Cosgrove, M. S. (2007) Histone proteomics and the epigenetic regulation of nucleosome mobility Expert Rev. Proteomics 4, 465-478
    • (2007) Expert Rev. Proteomics , vol.4 , pp. 465-478
    • Cosgrove, M.S.1
  • 5
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 A resolution Nature 389, 251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 6
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D. and Allis, C. D. (2000) The language of covalent histone modifications Nature 403, 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 7
    • 36448949026 scopus 로고    scopus 로고
    • Multivalent engagement of chromatin modifications by linked binding modules
    • Ruthenburg, A. J., Li, H., Patel, D. J., and Allis, C. D. (2007) Multivalent engagement of chromatin modifications by linked binding modules Nat. Rev. Mol. Cell Biol. 8, 983-994
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 983-994
    • Ruthenburg, A.J.1    Li, H.2    Patel, D.J.3    Allis, C.D.4
  • 8
    • 78149379276 scopus 로고    scopus 로고
    • Chemical tools in chromatin research
    • Schwarzer, D. (2010) Chemical tools in chromatin research J. Pept. Sci. 16, 530-537
    • (2010) J. Pept. Sci. , vol.16 , pp. 530-537
    • Schwarzer, D.1
  • 9
    • 83255192184 scopus 로고    scopus 로고
    • A peek into the complex realm of histone phosphorylation
    • Banerjee, T. and Chakravarti, D. (2011) A peek into the complex realm of histone phosphorylation Mol. Cell. Biol. 31, 4858-4873
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 4858-4873
    • Banerjee, T.1    Chakravarti, D.2
  • 10
    • 66449106900 scopus 로고    scopus 로고
    • Histone H3 phosphorylation: Universal code or lineage specific dialects?
    • Cerutti, H. and Casas-Mollano, J. A. (2009) Histone H3 phosphorylation: universal code or lineage specific dialects? Epigenetics 4, 71-75
    • (2009) Epigenetics , vol.4 , pp. 71-75
    • Cerutti, H.1    Casas-Mollano, J.A.2
  • 11
    • 0141613756 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3, what for?
    • Prigent, C. and Dimitrov, S. (2003) Phosphorylation of serine 10 in histone H3, what for? J. Cell Sci. 116, 3677-3685
    • (2003) J. Cell Sci. , vol.116 , pp. 3677-3685
    • Prigent, C.1    Dimitrov, S.2
  • 13
    • 38049018539 scopus 로고    scopus 로고
    • 14-3-3 proteins recognize a histone code at histone H3 and are required for transcriptional activation
    • Winter, S., Simboeck, E., Fischle, W., Zupkovitz, G., Dohnal, I., Mechtler, K., Ammerer, G., and Seiser, C. (2008) 14-3-3 proteins recognize a histone code at histone H3 and are required for transcriptional activation EMBO J. 27, 88-99
    • (2008) EMBO J. , vol.27 , pp. 88-99
    • Winter, S.1    Simboeck, E.2    Fischle, W.3    Zupkovitz, G.4    Dohnal, I.5    Mechtler, K.6    Ammerer, G.7    Seiser, C.8
  • 14
    • 42149189465 scopus 로고    scopus 로고
    • 14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation
    • Walter, W., Clynes, D., Tang, Y., Marmorstein, R., Mellor, J., and Berger, S. L. (2008) 14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation Mol. Cell. Biol. 28, 2840-2849
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 2840-2849
    • Walter, W.1    Clynes, D.2    Tang, Y.3    Marmorstein, R.4    Mellor, J.5    Berger, S.L.6
  • 15
    • 58049198236 scopus 로고    scopus 로고
    • Talk is cheap-cross-talk in establishment, maintenance, and readout of chromatin modifications
    • Fischle, W. (2008) Talk is cheap-cross-talk in establishment, maintenance, and readout of chromatin modifications Gene Dev. 22, 3375-3382
    • (2008) Gene Dev. , vol.22 , pp. 3375-3382
    • Fischle, W.1
  • 19
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R. and Mann, M. (2003) Mass spectrometry-based proteomics Nature 422, 198-207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 20
    • 84872085517 scopus 로고    scopus 로고
    • Systematic analysis of histone modification readout
    • Nikolov, M. and Fischle, W. (2013) Systematic analysis of histone modification readout Mol. BioSyst. 9, 182-194
    • (2013) Mol. BioSyst. , vol.9 , pp. 182-194
    • Nikolov, M.1    Fischle, W.2
  • 21
    • 78049246250 scopus 로고    scopus 로고
    • Fast signals and slow marks: The dynamics of histone modifications
    • Barth, T. K. and Imhof, A. (2010) Fast signals and slow marks: The dynamics of histone modifications Trends Biochem. Sci. 35, 618-626
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 618-626
    • Barth, T.K.1    Imhof, A.2
  • 23
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 24
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S. E. and Mann, M. (2006) A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC) Nat. Protoc. 1, 2650-2660
    • (2006) Nat. Protoc. , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 26
    • 0028882428 scopus 로고
    • Phosphonate inhibitors of protein-tyrosine and serine threonine phosphatases
    • Kole, H. K., Smyth, M. S., Russ, P. L., and Burke, T. R. (1995) Phosphonate inhibitors of protein-tyrosine and serine threonine phosphatases Biochem. J. 311, 1025-1031
    • (1995) Biochem. J. , vol.311 , pp. 1025-1031
    • Kole, H.K.1    Smyth, M.S.2    Russ, P.L.3    Burke, T.R.4
  • 28
    • 84862319345 scopus 로고    scopus 로고
    • Chemical biology techniques unlock the secrets of casein kinase 2 regulation by phosphorylation and glycosylation
    • Pavic, K. and Kohn, M. (2012) Chemical biology techniques unlock the secrets of casein kinase 2 regulation by phosphorylation and glycosylation ChemBioChem 13, 1253-1255
    • (2012) ChemBioChem , vol.13 , pp. 1253-1255
    • Pavic, K.1    Kohn, M.2
  • 29
    • 27744495195 scopus 로고    scopus 로고
    • Protein semisynthesis and expressed protein ligation: Chasing a protein's tail
    • Schwarzer, D. and Cole, P. A. (2005) Protein semisynthesis and expressed protein ligation: chasing a protein's tail Curr. Opin Chem. Biol. 9, 561-569
    • (2005) Curr. Opin Chem. Biol. , vol.9 , pp. 561-569
    • Schwarzer, D.1    Cole, P.A.2
  • 30
    • 33645473597 scopus 로고    scopus 로고
    • Negative regulation of a protein tyrosine phosphatase by tyrosine phosphorylation
    • Schwarzer, D., Zhang, Z. S., Zheng, W. P., and Cole, P. A. (2006) Negative regulation of a protein tyrosine phosphatase by tyrosine phosphorylation J. Am. Chem. Soc. 128, 4192-4193
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4192-4193
    • Schwarzer, D.1    Zhang, Z.S.2    Zheng, W.P.3    Cole, P.A.4
  • 32
    • 15444378543 scopus 로고    scopus 로고
    • Cellular stability of serotonin N-acetyltransferase conferred by phosphonodifluoromethylene alanine (Pfa) substitution for Ser-205
    • Zheng, W., Schwarzer, D., Lebeau, A., Weller, J. L., Klein, D. C., and Cole, P. A. (2005) Cellular stability of serotonin N-acetyltransferase conferred by phosphonodifluoromethylene alanine (Pfa) substitution for Ser-205 J. Biol. Chem. 280, 10462-10467
    • (2005) J. Biol. Chem. , vol.280 , pp. 10462-10467
    • Zheng, W.1    Schwarzer, D.2    Lebeau, A.3    Weller, J.L.4    Klein, D.C.5    Cole, P.A.6
  • 33
    • 0344628799 scopus 로고    scopus 로고
    • Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation
    • Zheng, W., Zhang, Z., Ganguly, S., Weller, J. L., Klein, D. C., and Cole, P. A. (2003) Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation Nat. Struct. Biol. 10, 1054-1057
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 1054-1057
    • Zheng, W.1    Zhang, Z.2    Ganguly, S.3    Weller, J.L.4    Klein, D.C.5    Cole, P.A.6
  • 34
    • 45749128943 scopus 로고    scopus 로고
    • Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patterns
    • Winter, S., Fischle, W., and Seiser, C. (2008) Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patterns Cell Cycle 7, 1336-1342
    • (2008) Cell Cycle , vol.7 , pp. 1336-1342
    • Winter, S.1    Fischle, W.2    Seiser, C.3
  • 35
    • 33746828109 scopus 로고    scopus 로고
    • Molecular recognition of histone H3 by the WD40 protein WDR5
    • Couture, J. F., Collazo, E., and Trievel, R. C. (2006) Molecular recognition of histone H3 by the WD40 protein WDR5 Nat. Struct. Mol. Biol. 13, 698-703
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 698-703
    • Couture, J.F.1    Collazo, E.2    Trievel, R.C.3
  • 36
    • 57749084606 scopus 로고    scopus 로고
    • Structure of WDR5 bound to mixed lineage leukemia protein-1 peptide
    • Patel, A., Dharmarajan, V., and Cosgrove, M. S. (2008) Structure of WDR5 bound to mixed lineage leukemia protein-1 peptide J. Biol. Chem. 283, 32158-32161
    • (2008) J. Biol. Chem. , vol.283 , pp. 32158-32161
    • Patel, A.1    Dharmarajan, V.2    Cosgrove, M.S.3
  • 37
    • 57749108294 scopus 로고    scopus 로고
    • A conserved arginine-containing motif crucial for the assembly and enzymatic activity of the mixed lineage leukemia protein-1 core complex
    • Patel, A., Vought, V. E., Dharmarajan, V., and Cosgrove, M. S. (2008) A conserved arginine-containing motif crucial for the assembly and enzymatic activity of the mixed lineage leukemia protein-1 core complex J. Biol. Chem. 283, 32162-32175
    • (2008) J. Biol. Chem. , vol.283 , pp. 32162-32175
    • Patel, A.1    Vought, V.E.2    Dharmarajan, V.3    Cosgrove, M.S.4
  • 39
    • 58049201719 scopus 로고    scopus 로고
    • WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket
    • Song, J. J. and Kingston, R. E. (2008) WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket J. Biol. Chem. 283, 35258-35264
    • (2008) J. Biol. Chem. , vol.283 , pp. 35258-35264
    • Song, J.J.1    Kingston, R.E.2
  • 40
    • 20444417108 scopus 로고    scopus 로고
    • WDR5 associates with histone H3 methylated at K4 and is essential for H3K4 methylation and vertebrate development
    • Wysocka, J., Swigut, T., Milne, T. A., Dou, Y. L., Zhang, X., Burlingame, A. L., Roeder, R. G., Brivanlou, A. H., and Allis, C. D. (2005) WDR5 associates with histone H3 methylated at K4 and is essential for H3K4 methylation and vertebrate development Cell 121, 859-872
    • (2005) Cell , vol.121 , pp. 859-872
    • Wysocka, J.1    Swigut, T.2    Milne, T.A.3    Dou, Y.L.4    Zhang, X.5    Burlingame, A.L.6    Roeder, R.G.7    Brivanlou, A.H.8    Allis, C.D.9
  • 42
    • 84857123708 scopus 로고    scopus 로고
    • Histone acetyltransferase 1: More than just an enzyme?
    • Parthun, M. R. (2012) Histone acetyltransferase 1: More than just an enzyme? Biochim. Biophys. Acta, Gene Regul. Mech. 1819, 256-263
    • (2012) Biochim. Biophys. Acta, Gene Regul. Mech. , vol.1819 , pp. 256-263
    • Parthun, M.R.1
  • 44
    • 0034529411 scopus 로고    scopus 로고
    • Paxillin interactions
    • Turner, C. E. (2000) Paxillin interactions J. Cell Sci. 113, 4139-4140
    • (2000) J. Cell Sci. , vol.113 , pp. 4139-4140
    • Turner, C.E.1
  • 45
    • 0038605975 scopus 로고    scopus 로고
    • FHL3 is an actin-binding protein that regulates alpha-actinin-mediated actin bundling - FHL3 localizes to actin stress fibers and enhances cell spreading and stress fiber disassembly
    • Coghill, I. D., Brown, S., Cottle, D. L., McGrath, M. J., Robinson, P. A., Nandurkar, H. H., Dyson, J. M., and Mitchell, C. A. (2003) FHL3 is an actin-binding protein that regulates alpha-actinin-mediated actin bundling-FHL3 localizes to actin stress fibers and enhances cell spreading and stress fiber disassembly J. Biol. Chem. 278, 24139-24152
    • (2003) J. Biol. Chem. , vol.278 , pp. 24139-24152
    • Coghill, I.D.1    Brown, S.2    Cottle, D.L.3    McGrath, M.J.4    Robinson, P.A.5    Nandurkar, H.H.6    Dyson, J.M.7    Mitchell, C.A.8
  • 46
    • 0032518442 scopus 로고    scopus 로고
    • Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase
    • Verreault, A., Kaufman, P. D., Kobayashi, R., and Stillman, B. (1998) Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase Curr. Biol. 8, 96-108
    • (1998) Curr. Biol. , vol.8 , pp. 96-108
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 47
    • 70350447999 scopus 로고    scopus 로고
    • Analysis of interaction partners of H4 histone by a new proteomics approach
    • Saade, E., Mechold, U., Kulyyassov, A., Vertut, D., Lipinski, M., and Ogryzko, V. (2009) Analysis of interaction partners of H4 histone by a new proteomics approach Proteomics 9, 4934-4943
    • (2009) Proteomics , vol.9 , pp. 4934-4943
    • Saade, E.1    Mechold, U.2    Kulyyassov, A.3    Vertut, D.4    Lipinski, M.5    Ogryzko, V.6
  • 48
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J. and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2


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