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Volumn 20, Issue 3, 2009, Pages 757-768

Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 3; PROTEIN BRE1; PROTEIN EBP1; PROTEIN P53; TRANSCRIPTION FACTOR E2F1; TUMOR SUPPRESSOR PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; E2F1 PROTEIN, HUMAN; ISOPROTEIN; PA2G4 PROTEIN, HUMAN; PHOSPHOSERINE; POLYUBIQUITIN; REPRESSOR PROTEIN; RNA BINDING PROTEIN; RNF40 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; UBIQUITIN PROTEIN LIGASE;

EID: 64049118773     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E08-09-0983     Document Type: Article
Times cited : (64)

References (49)
  • 1
    • 33646759590 scopus 로고    scopus 로고
    • Nuclear Akt associates with PKC-phosphorylated Ebpl, preventing DNA fragmentation by inhibition of caspase-activated DNase
    • Ahn, J. Y., Liu, X., Liu, Z., Pereira, L., Cheng, D., Peng, J., Wade, P. A., Hamburger, A. W., and Ye, K. (2006). Nuclear Akt associates with PKC-phosphorylated Ebpl, preventing DNA fragmentation by inhibition of caspase-activated DNase. EMBO J. 25, 2083-2095.
    • (2006) EMBO J , vol.25 , pp. 2083-2095
    • Ahn, J.Y.1    Liu, X.2    Liu, Z.3    Pereira, L.4    Cheng, D.5    Peng, J.6    Wade, P.A.7    Hamburger, A.W.8    Ye, K.9
  • 2
    • 35848940281 scopus 로고    scopus 로고
    • Ebpl-mediated inhibition of cell growth requires serine 363 phosphorylation
    • Akinmade, D., Lee, M., Zhang, Y., and Hamburger, A. W. (2007). Ebpl-mediated inhibition of cell growth requires serine 363 phosphorylation. Int. J. Oncol. 31, 851-858.
    • (2007) Int. J. Oncol , vol.31 , pp. 851-858
    • Akinmade, D.1    Lee, M.2    Zhang, Y.3    Hamburger, A.W.4
  • 4
    • 0036132855 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase Cdelta is essential for its apoptotic effect in response to etoposide
    • Blass, M., Kronfeld, I., Kazimirsky, G., Blumberg, P. M., and Brodie, C. (2002). Tyrosine phosphorylation of protein kinase Cdelta is essential for its apoptotic effect in response to etoposide. Mol. Cell. Biol. 22, 182-195.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 182-195
    • Blass, M.1    Kronfeld, I.2    Kazimirsky, G.3    Blumberg, P.M.4    Brodie, C.5
  • 5
    • 33646777450 scopus 로고    scopus 로고
    • Identification of Ebp1 as a component of cytoplasmic bcl-2 mRNP complexes
    • Bose, S. K., Sengupta, T. K., Bandyopadhyay, S., and Spicer, E. K. (2006). Identification of Ebp1 as a component of cytoplasmic bcl-2 mRNP complexes. Biochem. J. 396, 99-107.
    • (2006) Biochem. J , vol.396 , pp. 99-107
    • Bose, S.K.1    Sengupta, T.K.2    Bandyopadhyay, S.3    Spicer, E.K.4
  • 6
    • 13344260610 scopus 로고    scopus 로고
    • Bre1 is required for Notch signaling and histone modification
    • Bray, S., Musisi, H., and Bienz, M. (2005). Bre1 is required for Notch signaling and histone modification. Dev. Cell 8, 279-286.
    • (2005) Dev. Cell , vol.8 , pp. 279-286
    • Bray, S.1    Musisi, H.2    Bienz, M.3
  • 7
    • 21244451434 scopus 로고    scopus 로고
    • ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
    • Chen, D., Kon, N., Li, M., Zhang, W., Qin, J., and Gu, W. (2005). ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 121, 1071-1083.
    • (2005) Cell , vol.121 , pp. 1071-1083
    • Chen, D.1    Kon, N.2    Li, M.3    Zhang, W.4    Qin, J.5    Gu, W.6
  • 8
    • 24044547036 scopus 로고    scopus 로고
    • Regulating the regulators: Control of protein ubiquitination and ubiquitin-like modifications by extracellular stimuli
    • Gao, M., and Karin, M. (2005). Regulating the regulators: control of protein ubiquitination and ubiquitin-like modifications by extracellular stimuli. Mol. Cell 19, 581-593.
    • (2005) Mol. Cell , vol.19 , pp. 581-593
    • Gao, M.1    Karin, M.2
  • 12
    • 0037248593 scopus 로고    scopus 로고
    • A conserved RING finger protein required for histone H2B monoubiquitination and cell size control
    • Hwang, W. W., Venkatasubrahmanyam, S., Ianculescu, A. G., Tong, A., Boone, C., and Madhani, H. D. (2003). A conserved RING finger protein required for histone H2B monoubiquitination and cell size control. Mol. Cell 11, 261-266.
    • (2003) Mol. Cell , vol.11 , pp. 261-266
    • Hwang, W.W.1    Venkatasubrahmanyam, S.2    Ianculescu, A.G.3    Tong, A.4    Boone, C.5    Madhani, H.D.6
  • 13
    • 28444463638 scopus 로고    scopus 로고
    • The human homolog of yeast BRE1 functions as a transcriptional coactivator through direct activator interactions
    • Kim, J., Hake, S. B., and Roeder, R. G. (2005). The human homolog of yeast BRE1 functions as a transcriptional coactivator through direct activator interactions. Mol. Cell 20, 759-770.
    • (2005) Mol. Cell , vol.20 , pp. 759-770
    • Kim, J.1    Hake, S.B.2    Roeder, R.G.3
  • 14
    • 0034054236 scopus 로고    scopus 로고
    • Ectopic expression of the ErbB-3 binding protein ebp1 inhibits growth and induces differentiation of human breast cancer cell lines
    • Lessor, T. J., Yoo, J. Y., Xia, X., Woodford, N., and Hamburger, A. W. (2000). Ectopic expression of the ErbB-3 binding protein ebp1 inhibits growth and induces differentiation of human breast cancer cell lines. J. Cell. Physiol. 183 321-329.
    • (2000) J. Cell. Physiol , vol.183 , pp. 321-329
    • Lessor, T.J.1    Yoo, J.Y.2    Xia, X.3    Woodford, N.4    Hamburger, A.W.5
  • 15
    • 0035942177 scopus 로고    scopus 로고
    • Oncogenic ras activates the ARF-p53 pathway to suppress epithelial cell transformation
    • Lin, A. W., and Lowe, S. W. (2001). Oncogenic ras activates the ARF-p53 pathway to suppress epithelial cell transformation. Proc. Natl. Acad. Sci. USA 98, 5025-5030.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5025-5030
    • Lin, A.W.1    Lowe, S.W.2
  • 16
    • 33746660688 scopus 로고    scopus 로고
    • Ebp1 isoforms distinctively regulate cell survival and differentiation
    • Liu, Z., Ahn, J. Y., Liu, X., and Ye, K. (2006). Ebp1 isoforms distinctively regulate cell survival and differentiation. Proc. Natl. Acad. Sci. USA 103, 10917-10922.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10917-10922
    • Liu, Z.1    Ahn, J.Y.2    Liu, X.3    Ye, K.4
  • 17
    • 0034744224 scopus 로고    scopus 로고
    • Stabilization of p53 by p14ARF without relocation of MDM2 to the nucleolus
    • Llanos, S., Clark, P. A., Rowe, J., and Peters, G. (2001). Stabilization of p53 by p14ARF without relocation of MDM2 to the nucleolus. Nat. Cell Biol. 3, 445-452.
    • (2001) Nat. Cell Biol , vol.3 , pp. 445-452
    • Llanos, S.1    Clark, P.A.2    Rowe, J.3    Peters, G.4
  • 18
    • 0029952441 scopus 로고    scopus 로고
    • Maki, C. G., Huibregtse, J. M., and Howley, P. M. (1996). In vivo ubiquitination and proteasome-mediated degradation of p53(1). Cancer Res. 56, 26492654.
    • Maki, C. G., Huibregtse, J. M., and Howley, P. M. (1996). In vivo ubiquitination and proteasome-mediated degradation of p53(1). Cancer Res. 56, 26492654.
  • 19
    • 0030665146 scopus 로고    scopus 로고
    • Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53
    • Mayo, L. D., Turchi, J. J., and Berberich, S. J. (1997). Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53. Cancer Res. 57, 5013-5016.
    • (1997) Cancer Res , vol.57 , pp. 5013-5016
    • Mayo, L.D.1    Turchi, J.J.2    Berberich, S.J.3
  • 20
    • 0034603897 scopus 로고    scopus 로고
    • An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo
    • Midgley, C. A., Desterro, J. M., Saville, M. K., Howard, S., Sparks, A., Hay, R. T., and Lane, D. P. (2000). An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo. Oncogene 19, 2312-2323.
    • (2000) Oncogene , vol.19 , pp. 2312-2323
    • Midgley, C.A.1    Desterro, J.M.2    Saville, M.K.3    Howard, S.4    Sparks, A.5    Hay, R.T.6    Lane, D.P.7
  • 21
    • 0141483281 scopus 로고    scopus 로고
    • The Rtf1 component of the Paf1 transcriptional elongation complex is required for ubiquitination of histone H2B
    • Ng, H. H., Dole, S., and Struhl, K. (2003). The Rtf1 component of the Paf1 transcriptional elongation complex is required for ubiquitination of histone H2B. J. Biol. Chem. 278, 33625-33628.
    • (2003) J. Biol. Chem , vol.278 , pp. 33625-33628
    • Ng, H.H.1    Dole, S.2    Struhl, K.3
  • 22
    • 37549016788 scopus 로고    scopus 로고
    • Ebp1 association with nucleophos-min/b23 is essential for regulating cell proliferation and suppressing apoptosis
    • Okada, M., Jang, S. W., and Ye, K. (2007). Ebp1 association with nucleophos-min/b23 is essential for regulating cell proliferation and suppressing apoptosis. J. Biol. Chem. 282, 36744-36754.
    • (2007) J. Biol. Chem , vol.282 , pp. 36744-36754
    • Okada, M.1    Jang, S.W.2    Ye, K.3
  • 23
    • 1542298300 scopus 로고    scopus 로고
    • H2B ubiquitylation: The end is in sight
    • Osley, M. A. (2004). H2B ubiquitylation: the end is in sight. Biochim. Biophys. Acta 1677, 74-78.
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 74-78
    • Osley, M.A.1
  • 24
    • 33748304129 scopus 로고    scopus 로고
    • Quantitative profiling of drug-associated proteomic alterations by combined 2-nitrobenzenesulfenyl chloride (NBS) isotope labeling and 2DE/MS identification
    • Ou, K., et al. (2006). Quantitative profiling of drug-associated proteomic alterations by combined 2-nitrobenzenesulfenyl chloride (NBS) isotope labeling and 2DE/MS identification. J. Proteome Res. 5, 2194-2206.
    • (2006) J. Proteome Res , vol.5 , pp. 2194-2206
    • Ou, K.1
  • 25
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. (2001). Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 26
    • 0029165986 scopus 로고
    • Molecular cloning of a murine cDNA encoding a novel protein, p38-2G4, which varies with the cell cycle
    • Radomski, N., and Jost, E. (1995). Molecular cloning of a murine cDNA encoding a novel protein, p38-2G4, which varies with the cell cycle. Exp. Cell Res. 220, 434-445.
    • (1995) Exp. Cell Res , vol.220 , pp. 434-445
    • Radomski, N.1    Jost, E.2
  • 27
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk, K., Recht, J., and Osley, M. A. (2000). Rad6-dependent ubiquitination of histone H2B in yeast. Science 287, 501-504.
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 29
    • 34147107042 scopus 로고    scopus 로고
    • The homeobox gene CDX2 is aberrantly expressed in most cases of acute myeloid leukemia and promotes leukemogenesis
    • Scholl, C., et al. (2007). The homeobox gene CDX2 is aberrantly expressed in most cases of acute myeloid leukemia and promotes leukemogenesis. J. Clin. Invest. 117, 1037-1048.
    • (2007) J. Clin. Invest , vol.117 , pp. 1037-1048
    • Scholl, C.1
  • 30
    • 0035487104 scopus 로고    scopus 로고
    • The INK4a/ARF network in tumour suppression
    • Sherr, C. J. (2001). The INK4a/ARF network in tumour suppression. Nat. Rev. Mol. Cell Biol. 2, 731-737.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 731-737
    • Sherr, C.J.1
  • 31
    • 3042620165 scopus 로고    scopus 로고
    • EBP1 is a nucleolar growth-regulating protein that is part of pre-ribosomal ribonucleoprotein complexes
    • Squatrito, M., Mancino, M., Donzelli, M., Areces, L. B., and Draetta, G. F. (2004). EBP1 is a nucleolar growth-regulating protein that is part of pre-ribosomal ribonucleoprotein complexes. Oncogene 23, 4454-4465.
    • (2004) Oncogene , vol.23 , pp. 4454-4465
    • Squatrito, M.1    Mancino, M.2    Donzelli, M.3    Areces, L.B.4    Draetta, G.F.5
  • 32
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2 Bregulates H3 methylation and gene silencing in yeast
    • Sun, Z.W., and Allis, C.D.(2002).Ubiquitination of histone H2 Bregulates H3 methylation and gene silencing in yeast. Nature 418, 104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 33
    • 34848921532 scopus 로고    scopus 로고
    • Akt phosphorylation regulates the tumour-suppressor merlin through ubiquitination and degradation
    • Tang, X., Jang, S. W., Wang, X., Liu, Z., Bahr, S. M., Sun, S. Y., Brat, D., Gutmann, D. H., and Ye, K. (2007). Akt phosphorylation regulates the tumour-suppressor merlin through ubiquitination and degradation. Nat. Cell Biol. 9, 1199-1207.
    • (2007) Nat. Cell Biol , vol.9 , pp. 1199-1207
    • Tang, X.1    Jang, S.W.2    Wang, X.3    Liu, Z.4    Bahr, S.M.5    Sun, S.Y.6    Brat, D.7    Gutmann, D.H.8    Ye, K.9
  • 34
    • 33845977965 scopus 로고    scopus 로고
    • Ubiquitination regulates PTEN nuclear import and tumor suppression
    • Trotman, L. C., et al. (2007). Ubiquitination regulates PTEN nuclear import and tumor suppression. Cell 128, 141-156.
    • (2007) Cell , vol.128 , pp. 141-156
    • Trotman, L.C.1
  • 35
    • 33845991111 scopus 로고    scopus 로고
    • NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN
    • Wang, X. et al. (2007). NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN. Cell 128, 129-139.
    • (2007) Cell , vol.128 , pp. 129-139
    • Wang, X.1
  • 37
    • 0037248944 scopus 로고    scopus 로고
    • Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter
    • Wood, A., et al. (2003a). Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter. Mol. Cell 11, 267-274.
    • (2003) Mol. Cell , vol.11 , pp. 267-274
    • Wood, A.1
  • 38
    • 0042818412 scopus 로고    scopus 로고
    • The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p
    • Wood, A., Schneider, J., Dover, J., Johnston, M., and Shilatifard, A. (2003b). The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J. Biol. Chem. 278, 34739-34742.
    • (2003) J. Biol. Chem , vol.278 , pp. 34739-34742
    • Wood, A.1    Schneider, J.2    Dover, J.3    Johnston, M.4    Shilatifard, A.5
  • 39
    • 0035059136 scopus 로고    scopus 로고
    • Xia,X.,Cheng,A.,Lessor,T.,Zhang,Y.,andHamburger,A.W.(2001).Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb transcriptional regulation. J. Cell Physiol. 187, 209-217.
    • Xia,X.,Cheng,A.,Lessor,T.,Zhang,Y.,andHamburger,A.W.(2001).Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb transcriptional regulation. J. Cell Physiol. 187, 209-217.
  • 40
    • 0033637979 scopus 로고    scopus 로고
    • Pike. A nuclear GTPase that enhances PI3kinase activity and is regulated by protein 4.1N
    • Ye, K., Hurt, K. J., Wu, F. Y., Fang, M., Luo, H. R., Hong, J. J., Blackshaw, S., Ferris, C. D., and Snyder, S. H. (2000). Pike. A nuclear GTPase that enhances PI3kinase activity and is regulated by protein 4.1N. Cell 103, 919-930.
    • (2000) Cell , vol.103 , pp. 919-930
    • Ye, K.1    Hurt, K.J.2    Wu, F.Y.3    Fang, M.4    Luo, H.R.5    Hong, J.J.6    Blackshaw, S.7    Ferris, C.D.8    Snyder, S.H.9
  • 41
    • 0033980837 scopus 로고    scopus 로고
    • Interaction of the PA2G4 (EBP1) protein with ErbB-3 and regulation of this binding by heregulin
    • Yoo, J. Y., Wang, X. W., Rishi, A. K., Lessor, T., Xia, X. M., Gustafson, T. A., and Hamburger, A. W. (2000). Interaction of the PA2G4 (EBP1) protein with ErbB-3 and regulation of this binding by heregulin. Br. J. Cancer 82, 683-690.
    • (2000) Br. J. Cancer , vol.82 , pp. 683-690
    • Yoo, J.Y.1    Wang, X.W.2    Rishi, A.K.3    Lessor, T.4    Xia, X.M.5    Gustafson, T.A.6    Hamburger, A.W.7
  • 42
    • 33947222162 scopus 로고    scopus 로고
    • Suppression of salivary adenoid cystic carcinoma growth and metastasis by ErbB3 binding protein Ebp1 gene transfer
    • Yu, Y., Chen, W., Zhang, Y., Hamburger, A.W., Pan, H., and Zhang, Z. (2007). Suppression of salivary adenoid cystic carcinoma growth and metastasis by ErbB3 binding protein Ebp1 gene transfer. Int. J. Cancer 120, 1909-1913.
    • (2007) Int. J. Cancer , vol.120 , pp. 1909-1913
    • Yu, Y.1    Chen, W.2    Zhang, Y.3    Hamburger, A.W.4    Pan, H.5    Zhang, Z.6
  • 43
    • 27744544281 scopus 로고    scopus 로고
    • The ErbB3 binding protein Ebp1 interacts with Sin3A to repress E2F1 and AR-mediated transcription
    • Zhang, Y., Akinmade, D., and Hamburger, A. W. (2005a). The ErbB3 binding protein Ebp1 interacts with Sin3A to repress E2F1 and AR-mediated transcription. Nucleic Acids Res. 33, 6024-6033.
    • (2005) Nucleic Acids Res , vol.33 , pp. 6024-6033
    • Zhang, Y.1    Akinmade, D.2    Hamburger, A.W.3
  • 44
    • 0037103989 scopus 로고    scopus 로고
    • Repression of androgen receptor mediated transcription by the ErbB-3 binding protein, Ebp1
    • Zhang, Y., Fondell, J. D., Wang, Q., Xia, X., Cheng, A., Lu, M. L., and Hamburger, A. W. (2002). Repression of androgen receptor mediated transcription by the ErbB-3 binding protein, Ebp1. Oncogene 21, 5609-5618.
    • (2002) Oncogene , vol.21 , pp. 5609-5618
    • Zhang, Y.1    Fondell, J.D.2    Wang, Q.3    Xia, X.4    Cheng, A.5    Lu, M.L.6    Hamburger, A.W.7
  • 45
    • 13244283057 scopus 로고    scopus 로고
    • Specificity and heregulin regulation of Ebp1 (ErbB3 binding protein 1) mediated repression of androgen receptor signalling
    • Zhang, Y., and Hamburger, A. W. (2005). Specificity and heregulin regulation of Ebp1 (ErbB3 binding protein 1) mediated repression of androgen receptor signalling. Br. J. Cancer 92, 140-146.
    • (2005) Br. J. Cancer , vol.92 , pp. 140-146
    • Zhang, Y.1    Hamburger, A.W.2
  • 47
    • 0038813929 scopus 로고    scopus 로고
    • Zhang,Y.,Woodford,N.,Xia,X.,andHamburger,A.W.(2003).Repressionof E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases. Nucleic Acids Res. 31, 2168-2177.
    • Zhang,Y.,Woodford,N.,Xia,X.,andHamburger,A.W.(2003).Repressionof E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases. Nucleic Acids Res. 31, 2168-2177.
  • 48
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • Zhong, Q., Gao, W., Du, F., and Wang, X. (2005). Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 121, 1085-1095.
    • (2005) Cell , vol.121 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4
  • 49
    • 27944454433 scopus 로고    scopus 로고
    • Monoubiquitination of human histone H2B: The factors involved and their roles in HOX gene regulation
    • Zhu, B., Zheng, Y., Pham, A. D., Mandal, S. S., Erdjument-Bromage, H., Tempst, P., and Reinberg, D. (2005). Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation. Mol. Cell 20, 601-611.
    • (2005) Mol. Cell , vol.20 , pp. 601-611
    • Zhu, B.1    Zheng, Y.2    Pham, A.D.3    Mandal, S.S.4    Erdjument-Bromage, H.5    Tempst, P.6    Reinberg, D.7


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