메뉴 건너뛰기




Volumn 15, Issue 4, 2004, Pages 573-584

Chromosomal protein HMGN1 modulates histone H3 phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ANISOMYCIN; CHROMOSOME PROTEIN; HIGH MOBILITY GROUP N1 PROTEIN; HISTONE H3; NUCLEAR PROTEIN;

EID: 4344643548     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.08.006     Document Type: Article
Times cited : (106)

References (37)
  • 1
    • 0028274720 scopus 로고
    • The footprint of chromosomal proteins HMG-14 and HMG-17 on chromatin subunits
    • Alfonso P.J., Crippa M.P., Hayes J.J., Bustin M. The footprint of chromosomal proteins HMG-14 and HMG-17 on chromatin subunits. J. Mol. Biol. 236:1994;189-198
    • (1994) J. Mol. Biol. , vol.236 , pp. 189-198
    • Alfonso, P.J.1    Crippa, M.P.2    Hayes, J.J.3    Bustin, M.4
  • 2
    • 0027941473 scopus 로고
    • A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in its basic amino-terminal domain in vivo and on isolated mononucleosomes
    • Barratt M.J., Hazzalin C.A., Zhelev N., Mahadevan L.C. A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in its basic amino-terminal domain in vivo and on isolated mononucleosomes. EMBO J. 13:1994;4524-4535
    • (1994) EMBO J. , vol.13 , pp. 4524-4535
    • Barratt, M.J.1    Hazzalin, C.A.2    Zhelev, N.3    Mahadevan, L.C.4
  • 4
    • 0025445881 scopus 로고
    • Growth factor-responsive genes in fibroblasts
    • Bravo R. Growth factor-responsive genes in fibroblasts. Cell Growth Differ. 1:1990;305-309
    • (1990) Cell Growth Differ. , vol.1 , pp. 305-309
    • Bravo, R.1
  • 5
    • 0035399963 scopus 로고    scopus 로고
    • Chromatin unfolding and activation by HMGN(*) chromosomal proteins
    • Bustin M. Chromatin unfolding and activation by HMGN(*) chromosomal proteins. Trends Biochem. Sci. 26:2001;431-437
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 431-437
    • Bustin, M.1
  • 6
    • 0036668636 scopus 로고    scopus 로고
    • Competition between histone H1 and HMGN proteins for chromatin binding sites
    • Catez F., Brown D.T., Misteli T., Bustin M. Competition between histone H1 and HMGN proteins for chromatin binding sites. EMBO Rep. 3:2002;760-766
    • (2002) EMBO Rep. , vol.3 , pp. 760-766
    • Catez, F.1    Brown, D.T.2    Misteli, T.3    Bustin, M.4
  • 8
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P., Allis C.D., Sassone-Corsi P. Signaling to chromatin through histone modifications. Cell. 103:2000;263-271
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 9
    • 0038538472 scopus 로고    scopus 로고
    • MAP kinase-mediated phosphoacetylation of histone H3 and inducible gene regulation
    • Clayton A.L., Mahadevan L.C. MAP kinase-mediated phosphoacetylation of histone H3 and inducible gene regulation. FEBS Lett. 546:2003;51-58
    • (2003) FEBS Lett. , vol.546 , pp. 51-58
    • Clayton, A.L.1    Mahadevan, L.C.2
  • 10
    • 0034679625 scopus 로고    scopus 로고
    • Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation
    • Clayton A.L., Rose S., Barratt M.J., Mahadevan L.C. Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation. EMBO J. 19:2000;3714-3726
    • (2000) EMBO J. , vol.19 , pp. 3714-3726
    • Clayton, A.L.1    Rose, S.2    Barratt, M.J.3    Mahadevan, L.C.4
  • 11
    • 0026676799 scopus 로고
    • Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain
    • Crippa M.P., Alfonso P.J., Bustin M. Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain. J. Mol. Biol. 228:1992;442-449
    • (1992) J. Mol. Biol. , vol.228 , pp. 442-449
    • Crippa, M.P.1    Alfonso, P.J.2    Bustin, M.3
  • 12
    • 0041975981 scopus 로고    scopus 로고
    • MSK1 and MSK2 mediate mitogen- and stress-induced phosphorylation of histone H3: A controversy resolved
    • PE33.
    • Davie, J.R. (2003). MSK1 and MSK2 mediate mitogen- and stress-induced phosphorylation of histone H3: a controversy resolved. Sci. STKE 2003, PE33.
    • (2003) Sci. STKE 2003
    • Davie, J.R.1
  • 13
    • 35848958631 scopus 로고    scopus 로고
    • Signal transduction pathways and the modification of chromatin structure
    • Davie J.R., Spencer V.A. Signal transduction pathways and the modification of chromatin structure. Prog. Nucleic Acid Res. Mol. Biol. 65:2001;299-340
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.65 , pp. 299-340
    • Davie, J.R.1    Spencer, V.A.2
  • 15
    • 0031896910 scopus 로고    scopus 로고
    • Anisomycin selectively desensitizes signalling components involved in stress kinase activation and fos and jun induction
    • Hazzalin C.A., Le Panse R., Cano E., Mahadevan L.C. Anisomycin selectively desensitizes signalling components involved in stress kinase activation and fos and jun induction. Mol. Cell. Biol. 18:1998;1844-1854
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1844-1854
    • Hazzalin, C.A.1    Le Panse, R.2    Cano, E.3    Mahadevan, L.C.4
  • 16
    • 0032933141 scopus 로고    scopus 로고
    • Specific acetylation of chromosomal protein HMG-17 by P/CAF alters its interaction with nucleosomes
    • Herrera J., Sakaguchi K., Bergel M., Trieschmann L., Nakatani Y., Bustin M. Specific acetylation of chromosomal protein HMG-17 by P/CAF alters its interaction with nucleosomes. Mol. Cell. Biol. 19:1999;3466-3473
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3466-3473
    • Herrera, J.1    Sakaguchi, K.2    Bergel, M.3    Trieschmann, L.4    Nakatani, Y.5    Bustin, M.6
  • 19
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., 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
  • 20
    • 0037229898 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 during transcriptional activation depends on promoter structure
    • Labrador M., Corces V.G. Phosphorylation of histone H3 during transcriptional activation depends on promoter structure. Genes Dev. 17:2003;43-48
    • (2003) Genes Dev. , vol.17 , pp. 43-48
    • Labrador, M.1    Corces, V.G.2
  • 22
    • 0033979602 scopus 로고    scopus 로고
    • Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry
    • Louie D.F., Gloor K.K., Galasinski S.C., Resing K.A., Ahn N.G. Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry. Protein Sci. 9:2000;170-179
    • (2000) Protein Sci. , vol.9 , pp. 170-179
    • Louie, D.F.1    Gloor, K.K.2    Galasinski, S.C.3    Resing, K.A.4    Ahn, N.G.5
  • 23
    • 0025872683 scopus 로고
    • Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors
    • Mahadevan L.C., Willis A.C., Barratt M.J. Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors. Cell. 65:1991;775-783
    • (1991) Cell , vol.65 , pp. 775-783
    • Mahadevan, L.C.1    Willis, A.C.2    Barratt, M.J.3
  • 26
    • 0036785555 scopus 로고    scopus 로고
    • Mitotic phosphorylation of chromosomal protein HMGN1 inhibits nuclear import and promotes interaction with 14.3.3 proteins
    • Prymakowska-Bosak M., Hock R., Catez F., Lim J.H., Birger Y., Shirakawa H., Lee K., Bustin M. Mitotic phosphorylation of chromosomal protein HMGN1 inhibits nuclear import and promotes interaction with 14.3.3 proteins. Mol. Cell. Biol. 22:2002;6809-6819
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6809-6819
    • Prymakowska-Bosak, M.1    Hock, R.2    Catez, F.3    Lim, J.H.4    Birger, Y.5    Shirakawa, H.6    Lee, K.7    Bustin, M.8
  • 27
    • 0019322514 scopus 로고
    • The interaction of high mobility proteins HMG14 and 17 with nucleosomes
    • Sandeen G., Wood W.I., Felsenfeld G. The interaction of high mobility proteins HMG14 and 17 with nucleosomes. Nucleic Acids Res. 8:1980;3757-3778
    • (1980) Nucleic Acids Res. , vol.8 , pp. 3757-3778
    • Sandeen, G.1    Wood, W.I.2    Felsenfeld, G.3
  • 29
    • 0027247780 scopus 로고
    • Cell cycle-dependent suppressive effect of histone H1 on mitosis-specific H3 phosphorylation
    • Shibata K., Ajiro K. Cell cycle-dependent suppressive effect of histone H1 on mitosis-specific H3 phosphorylation. J. Biol. Chem. 268:1993;18431-18434
    • (1993) J. Biol. Chem. , vol.268 , pp. 18431-18434
    • Shibata, K.1    Ajiro, K.2
  • 31
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., Allis C.D. The language of covalent histone modifications. Nature. 403:2000;41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 32
    • 0033200205 scopus 로고    scopus 로고
    • The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase
    • a
    • Thomson S., Clayton A.L., Hazzalin C.A., Rose S., Barratt M.J., Mahadevan L.C. The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades. MSK1 as a potential histone H3/HMG-14 kinase EMBO J. 18:1999;4779-4793. a
    • (1999) EMBO J. , vol.18 , pp. 4779-4793
    • Thomson, S.1    Clayton, A.L.2    Hazzalin, C.A.3    Rose, S.4    Barratt, M.J.5    Mahadevan, L.C.6
  • 33
    • 0033113010 scopus 로고    scopus 로고
    • MAP kinase-mediated signalling to nucleosomes and immediate-early gene induction
    • b
    • Thomson S., Mahadevan L.C., Clayton A.L. MAP kinase-mediated signalling to nucleosomes and immediate-early gene induction. Semin. Cell Dev. Biol. 10:1999;205-214. b
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 205-214
    • Thomson, S.1    Mahadevan, L.C.2    Clayton, A.L.3
  • 34
    • 0028791878 scopus 로고
    • Modular structure of chromosomal proteins HMG-14 and HMG-17: Definition of a transcriptional activation domain distinct from the nucleosomal binding domain
    • Trieschmann L., Postnikov Y., Rickers A., Bustin M. Modular structure of chromosomal proteins HMG-14 and HMG-17. definition of a transcriptional activation domain distinct from the nucleosomal binding domain Mol. Cell. Biol. 15:1995;6663-6669
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6663-6669
    • Trieschmann, L.1    Postnikov, Y.2    Rickers, A.3    Bustin, M.4
  • 35
    • 0032510746 scopus 로고    scopus 로고
    • The chromatin unfolding domain of chromosomal protein HMG-14 targets the N-terminal tail of histone H3 in nucleosomes
    • Trieschmann L., Martin B., Bustin M. The chromatin unfolding domain of chromosomal protein HMG-14 targets the N-terminal tail of histone H3 in nucleosomes. Proc. Natl. Acad. Sci. USA. 95:1998;5468-5473
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5468-5473
    • Trieschmann, L.1    Martin, B.2    Bustin, M.3
  • 36
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner B.M. Cellular memory and the histone code. Cell. 111:2002;285-291
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 37
    • 0038511129 scopus 로고    scopus 로고
    • Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression
    • Yamamoto Y., Verma U.N., Prajapati S., Kwak Y.T., Gaynor R.B. Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression. Nature. 423:2003;655-659
    • (2003) Nature , vol.423 , pp. 655-659
    • Yamamoto, Y.1    Verma, U.N.2    Prajapati, S.3    Kwak, Y.T.4    Gaynor, R.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.