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Volumn 11, Issue 7, 2004, Pages 747-759

E2FBP1/hDril1 modulates cell growth through downregulation of promyelocytic leukemia bodies

Author keywords

PML nuclear body; Premature senescence; Protein protein interaction; Sumoylation

Indexed keywords

ADENINE; DNA BINDING PROTEIN; DRIL1 PROTEIN; THYMINE; TRANSCRIPTION FACTOR E2F BINDING PROTEIN 1; UNCLASSIFIED DRUG;

EID: 3543097985     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401412     Document Type: Article
Times cited : (19)

References (36)
  • 1
  • 2
    • 0032528049 scopus 로고    scopus 로고
    • The human dead ringer/bright homolog, DRIL1: cDNA cloning, gene structure, and mapping to D19S886, a marker on 19p13.3 that is strictly linked to the Peutz-Jeghers syndrome
    • Kortschak RD, Reimann H, Zimmer M, Eyre HJ, Saint R and Jenne DE (1998) The human dead ringer/bright homolog, DRIL1: cDNA cloning, gene structure, and mapping to D19S886, a marker on 19p13.3 that is strictly linked to the Peutz-Jeghers syndrome. Genomics 51: 288-292
    • (1998) Genomics , vol.51 , pp. 288-292
    • Kortschak, R.D.1    Reimann, H.2    Zimmer, M.3    Eyre, H.J.4    Saint, R.5    Jenne, D.E.6
  • 4
    • 0030657575 scopus 로고    scopus 로고
    • Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9
    • Gong L, Kamitani T, Fujise K, Caskey LS and Yeh ET (1997) Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9. J. Biol. Chem. 272: 28198-28201
    • (1997) J. Biol. Chem. , vol.272 , pp. 28198-28201
    • Gong, L.1    Kamitani, T.2    Fujise, K.3    Caskey, L.S.4    Yeh, E.T.5
  • 5
    • 0034254161 scopus 로고    scopus 로고
    • Regulation of matrix attachment region-dependent, lymphocyte-restricted transcription through differential localization within promyelocytic leukemia nuclear bodies
    • Zong RT, Das C and Tucker PW (2000) Regulation of matrix attachment region-dependent, lymphocyte-restricted transcription through differential localization within promyelocytic leukemia nuclear bodies. EMBO J. 19: 4123-4133
    • (2000) EMBO J. , vol.19 , pp. 4123-4133
    • Zong, R.T.1    Das, C.2    Tucker, P.W.3
  • 6
    • 0034836386 scopus 로고    scopus 로고
    • The transcription factor, Bright, and immunoglobulin heavy chain expression
    • Webb CF (2001) The transcription factor, Bright, and immunoglobulin heavy chain expression. Immunol. Res. 24: 149-161
    • (2001) Immunol. Res. , vol.24 , pp. 149-161
    • Webb, C.F.1
  • 7
    • 0029610034 scopus 로고
    • The immunoglobulin heavy-chain matrix-associating regions are bound by Bright: A B cell-specific trans-activator that describes a new DNA-binding protein family
    • Herrscher RF, Kaplan MH, Lelsz DL, Das C, Scheuermann R and Tucker PW (1995) The immunoglobulin heavy-chain matrix-associating regions are bound by Bright: a B cell-specific trans-activator that describes a new DNA-binding protein family. Genes Dev. 9: 3067-3082
    • (1995) Genes Dev. , vol.9 , pp. 3067-3082
    • Herrscher, R.F.1    Kaplan, M.H.2    Lelsz, D.L.3    Das, C.4    Scheuermann, R.5    Tucker, P.W.6
  • 8
    • 0036318221 scopus 로고    scopus 로고
    • Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions for PML nuclear bodies
    • Borden KL (2002) Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies. Mol. Cell Biol. 22: 5259-5269
    • (2002) Mol. Cell Biol. , vol.22 , pp. 5259-5269
    • Borden, K.L.1
  • 9
    • 0033925534 scopus 로고    scopus 로고
    • Review: Properties and assembly mechanisms of ND10, PMIL bodies, or PODs
    • Maul GG, Negorev D, Bell P and Ishov AM (2000) Review: properties and assembly mechanisms of ND10, PMIL bodies, or PODs. J. Struct. Biol. 129: 278-287
    • (2000) J. Struct. Biol. , vol.129 , pp. 278-287
    • Maul, G.G.1    Negorev, D.2    Bell, P.3    Ishov, A.M.4
  • 10
    • 0035969107 scopus 로고    scopus 로고
    • Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot
    • Negorev D and Maul GG (2001) Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene 20: 7234-7242
    • (2001) Oncogene , vol.20 , pp. 7234-7242
    • Negorev, D.1    Maul, G.G.2
  • 11
    • 0033152703 scopus 로고    scopus 로고
    • The PML nuclear bodies: Actors or extras?
    • Seeler JS and Dejean A (1999) The PML nuclear bodies: actors or extras? Curr. Opin. Genet. Dev. 9: 362-367
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 362-367
    • Seeler, J.S.1    Dejean, A.2
  • 12
    • 0035986065 scopus 로고    scopus 로고
    • The promyelocytic leukemia nuclear body: Sites of activity?
    • Eskiw CH and Bazett-Jones DP (2002) The promyelocytic leukemia nuclear body: sites of activity? Biochem. Cell Biol. 80: 301-310
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 301-310
    • Eskiw, C.H.1    Bazett-Jones, D.P.2
  • 13
    • 0035969104 scopus 로고    scopus 로고
    • PML interaction with p53 and its role in apoptosis and replicative senescence
    • Pearson M and Pelicci PG (2001) PML interaction with p53 and its role in apoptosis and replicative senescence. Oncogene 20: 7250-7256
    • (2001) Oncogene , vol.20 , pp. 7250-7256
    • Pearson, M.1    Pelicci, P.G.2
  • 14
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni P and Pandolfi PP (2002) The role of PML in tumor suppression. Cell 108: 165-170
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 15
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett RD (2001) DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20: 7266-7273
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 16
    • 0035969099 scopus 로고    scopus 로고
    • Orchestration of multiple arrays of signal cross-talk and combinatorial interactions for maturation and cell death: Another vision of t(15;17) preleukemic blast and APL-cell maturation
    • Benoit G, Roussel M, Pendino F, Segal-Bendirdjian E and Lanotte M (2001) Orchestration of multiple arrays of signal cross-talk and combinatorial interactions for maturation and cell death: another vision of t(15;17) preleukemic blast and APL-cell maturation. Oncogene 20: 7161-7177
    • (2001) Oncogene , vol.20 , pp. 7161-7177
    • Benoit, G.1    Roussel, M.2    Pendino, F.3    Segal-Bendirdjian, E.4    Lanotte, M.5
  • 19
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James P, Halladay J and Craig EA (1996) Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144: 1425-1436
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 21
    • 0033380850 scopus 로고    scopus 로고
    • Cell cycle regulation of PML modification and ND10 composition
    • Everett RD, Lomonte P, Sternsdorf T, van Driel R and Orr A (1999) Cell cycle regulation of PML modification and ND10 composition. J. Cell Sci. 112 (Part 24): 4581-4588
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 24 , pp. 4581-4588
    • Everett, R.D.1    Lomonte, P.2    Sternsdorf, T.3    van Driel, R.4    Orr, A.5
  • 27
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li S-J and Hochstrasser M (1999) A new protease required for cell-cycle progression in yeast. Nature 398: 246-251
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.-J.1    Hochstrasser, M.2
  • 28
    • 0037062951 scopus 로고    scopus 로고
    • RNA interference
    • Hannon GJ (2002) RNA interference. Nature 418: 244-251
    • (2002) Nature , vol.418 , pp. 244-251
    • Hannon, G.J.1
  • 30
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • Serrano M, Lin AW, McCurrach ME, Beach D and Lowe SW (1997) Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88: 593-602
    • (1997) Cell , vol.88 , pp. 593-602
    • Serrano, M.1    Lin, A.W.2    McCurrach, M.E.3    Beach, D.4    Lowe, S.W.5
  • 32
    • 0037979238 scopus 로고    scopus 로고
    • PML colocalizes with and stabilizes the DNA damage response protein TopBP1
    • Xu ZX, Timanova-Atanasova A, Zhao RX and Chang KS (2003) PML colocalizes with and stabilizes the DNA damage response protein TopBP1. Mol. Cell Biol. 23: 4247-4256
    • (2003) Mol. Cell Biol. , vol.23 , pp. 4247-4256
    • Xu, Z.X.1    Timanova-Atanasova, A.2    Zhao, R.X.3    Chang, K.S.4
  • 33
    • 0000269420 scopus 로고    scopus 로고
    • Immunoaffinity purification
    • 1st edn. (New York: Cold Spring Harbor Laboratory)
    • Harlow E and Lane D (1999) Immunoaffinity purification. In Using Antibodies; A Laboratory Manual, 1st edn. (New York: Cold Spring Harbor Laboratory) pp. 311-343
    • (1999) Using Antibodies; A Laboratory Manual , pp. 311-343
    • Harlow, E.1    Lane, D.2
  • 34
    • 0035877642 scopus 로고    scopus 로고
    • Transcriptional activation by a matrix associating region-binding protein. Contextual requirements for the function of bright
    • Kaplan MH, Zong RT, Henscher RF, Scheuermann RH and Tucker PW (2001) Transcriptional activation by a matrix associating region-binding protein. Contextual requirements for the function of bright. J. Biol. Chem. 276: 21325-21330
    • (2001) J. Biol. Chem. , vol.276 , pp. 21325-21330
    • Kaplan, M.H.1    Zong, R.T.2    Henscher, R.F.3    Scheuermann, R.H.4    Tucker, P.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.