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Volumn 582, Issue 23-24, 2008, Pages 3257-3262

The promiscuity of ARF interactions with the proteasome

Author keywords

Cell stress sensor; p14 p19ARF; Proteasome; REG ; TBP 1 PSMC3

Indexed keywords

ARF PROTEIN; CYCLIN DEPENDENT KINASE INHIBITOR 2D; PROTEASOME; PROTEIN P14; TRANSCRIPTION FACTOR E2F; TRANSCRIPTION FACTOR E2F1; TUMOR SUPPRESSOR PROTEIN;

EID: 53049106860     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.09.026     Document Type: Short Survey
Times cited : (24)

References (69)
  • 1
    • 0037309326 scopus 로고    scopus 로고
    • Tumor suppression by Ink4a-Arf: progress and puzzles
    • Lowe S.W., and Sherr C.J. Tumor suppression by Ink4a-Arf: progress and puzzles. Curr. Opin. Genet. Dev. 13 (2003) 77-83
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 77-83
    • Lowe, S.W.1    Sherr, C.J.2
  • 2
    • 33747819484 scopus 로고    scopus 로고
    • Divorcing ARF and p53: an unsettled case
    • Sherr C.J. Divorcing ARF and p53: an unsettled case. Nat. Rev. Cancer 6 (2006) 663-673
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 663-673
    • Sherr, C.J.1
  • 3
    • 33646861005 scopus 로고    scopus 로고
    • p14ARF activates a Tip60-dependent and p53-independent ATM/ATR/CHK pathway in response to genotoxic stress
    • Eymin B., Claverie P., Salon C., Leduc C., Col E., Brambilla E., Khochbin S., and Gazzeri S. p14ARF activates a Tip60-dependent and p53-independent ATM/ATR/CHK pathway in response to genotoxic stress. Mol. Cell Biol. 26 (2006) 4339-4350
    • (2006) Mol. Cell Biol. , vol.26 , pp. 4339-4350
    • Eymin, B.1    Claverie, P.2    Salon, C.3    Leduc, C.4    Col, E.5    Brambilla, E.6    Khochbin, S.7    Gazzeri, S.8
  • 4
    • 0035958932 scopus 로고    scopus 로고
    • The p14ARF tumor suppressor protein facilitates nucleolar sequestration of hypoxia-inducible factor-1alpha (HIF-1alpha) and inhibits HIF-1-mediated transcription
    • Fatyol K., and Szalay A.A. The p14ARF tumor suppressor protein facilitates nucleolar sequestration of hypoxia-inducible factor-1alpha (HIF-1alpha) and inhibits HIF-1-mediated transcription. J. Biol. Chem. 276 (2001) 28421-28429
    • (2001) J. Biol. Chem. , vol.276 , pp. 28421-28429
    • Fatyol, K.1    Szalay, A.A.2
  • 5
    • 33748937018 scopus 로고    scopus 로고
    • Antiviral action of the tumor suppressor ARF
    • Garcia M.A., et al. Antiviral action of the tumor suppressor ARF. EMBO J. 25 (2006) 4284-4292
    • (2006) EMBO J. , vol.25 , pp. 4284-4292
    • Garcia, M.A.1
  • 9
    • 0041662272 scopus 로고    scopus 로고
    • Integration of interferon-alpha/beta signalling to p53 responses in tumour suppression and antiviral defence
    • Takaoka A., et al. Integration of interferon-alpha/beta signalling to p53 responses in tumour suppression and antiviral defence. Nature 424 (2003) 516-523
    • (2003) Nature , vol.424 , pp. 516-523
    • Takaoka, A.1
  • 10
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: a suitable antineoplastic target
    • Adams. The proteasome: a suitable antineoplastic target. Nat. Rev. Cancer 4 (2004) 349-360
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 349-360
    • Adams1
  • 12
    • 13244275245 scopus 로고    scopus 로고
    • A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73
    • Asher G., Tsvetkov P., Kahana C., and Shaul Y. A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73. Genes Dev. 19 (2005) 316-321
    • (2005) Genes Dev. , vol.19 , pp. 316-321
    • Asher, G.1    Tsvetkov, P.2    Kahana, C.3    Shaul, Y.4
  • 13
    • 0029068172 scopus 로고
    • Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26S proteasome
    • Jariel-Encontre I P.M., Martin F., Carillo S., Salvat C., and Piechaczyk M. Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26S proteasome. J. Biol. Chem. 270 (1995) 11623-11627
    • (1995) J. Biol. Chem. , vol.270 , pp. 11623-11627
    • Jariel-Encontre I, P.M.1    Martin, F.2    Carillo, S.3    Salvat, C.4    Piechaczyk, M.5
  • 14
    • 0037452979 scopus 로고    scopus 로고
    • Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein
    • Kalejta R.F., and Shenk T. Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein. Proc. Natl. Acad. Sci. USA 100 (2003) 3263-3268
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3263-3268
    • Kalejta, R.F.1    Shenk, T.2
  • 15
    • 0026669739 scopus 로고
    • Identification, purification, and characterization of a protein activator (PA28) of the 20S proteasome (macropain)
    • Ma C.P., Slaughter C.A., and DeMartino G.N. Identification, purification, and characterization of a protein activator (PA28) of the 20S proteasome (macropain). J. Biol. Chem. 267 (1992) 10515-10523
    • (1992) J. Biol. Chem. , vol.267 , pp. 10515-10523
    • Ma, C.P.1    Slaughter, C.A.2    DeMartino, G.N.3
  • 19
    • 40549097029 scopus 로고    scopus 로고
    • REGgamma proteasome activator is involved in the maintenance of chromosomal stability
    • Zannini L., et al. REGgamma proteasome activator is involved in the maintenance of chromosomal stability. Cell Cycle 7 (2008) 504-512
    • (2008) Cell Cycle , vol.7 , pp. 504-512
    • Zannini, L.1
  • 20
    • 3543148255 scopus 로고    scopus 로고
    • N-terminal polyubiquitination and degradation of the Arf tumor suppressor
    • Kuo M.L., den Besten W., Bertwistle D., Roussel M.F., and Sherr C.J. N-terminal polyubiquitination and degradation of the Arf tumor suppressor. Genes Dev. 18 (2004) 1862-1874
    • (2004) Genes Dev. , vol.18 , pp. 1862-1874
    • Kuo, M.L.1    den Besten, W.2    Bertwistle, D.3    Roussel, M.F.4    Sherr, C.J.5
  • 21
    • 4344702484 scopus 로고    scopus 로고
    • Stability of nucleolar versus non-nucleolar forms of human p14(ARF)
    • Rodway H., Llanos S., Rowe J., and Peters G. Stability of nucleolar versus non-nucleolar forms of human p14(ARF). Oncogene 23 (2004) 6186-6192
    • (2004) Oncogene , vol.23 , pp. 6186-6192
    • Rodway, H.1    Llanos, S.2    Rowe, J.3    Peters, G.4
  • 22
    • 34250342888 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome
    • Chen X., Barton L.F., Chi Y., Clurman B.E., and Roberts J.M. Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome. Mol. Cell. 26 (2007) 843-852
    • (2007) Mol. Cell. , vol.26 , pp. 843-852
    • Chen, X.1    Barton, L.F.2    Chi, Y.3    Clurman, B.E.4    Roberts, J.M.5
  • 23
    • 33846928412 scopus 로고    scopus 로고
    • Specific amino acid residues in the basic helix-loop-helix domain of SRC-3 are essential for its nuclear localization and proteasome-dependent turnover
    • Li C., Wu R.C., Amazit L., Tsai S.Y., Tsai M.J., and O'Malley B.W. Specific amino acid residues in the basic helix-loop-helix domain of SRC-3 are essential for its nuclear localization and proteasome-dependent turnover. Mol. Cell. Biol. 27 (2007) 1296-1308
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1296-1308
    • Li, C.1    Wu, R.C.2    Amazit, L.3    Tsai, S.Y.4    Tsai, M.J.5    O'Malley, B.W.6
  • 24
    • 31044439969 scopus 로고    scopus 로고
    • REGgamma: a shortcut to destruction
    • Zhou P. REGgamma: a shortcut to destruction. Cell 124 (2006) 256-257
    • (2006) Cell , vol.124 , pp. 256-257
    • Zhou, P.1
  • 25
    • 4744371446 scopus 로고    scopus 로고
    • The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct evidence for ubiquitination at the N-terminal residue
    • Ben-Saadon R., Fajerman I., Ziv T., Hellman U., Schwartz A.L., and Ciechanover A. The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct evidence for ubiquitination at the N-terminal residue. J. Biol. Chem. 279 (2004) 41414-41421
    • (2004) J. Biol. Chem. , vol.279 , pp. 41414-41421
    • Ben-Saadon, R.1    Fajerman, I.2    Ziv, T.3    Hellman, U.4    Schwartz, A.L.5    Ciechanover, A.6
  • 26
    • 14644401017 scopus 로고    scopus 로고
    • N-Terminal polyubiquitination of the ARF tumor suppressor, a natural lysine-less protein
    • Kuo M.L., den Besten W., and Sherr C.J. N-Terminal polyubiquitination of the ARF tumor suppressor, a natural lysine-less protein. Cell Cycle 3 (2004) 1367-1369
    • (2004) Cell Cycle , vol.3 , pp. 1367-1369
    • Kuo, M.L.1    den Besten, W.2    Sherr, C.J.3
  • 27
    • 31044449824 scopus 로고    scopus 로고
    • The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome
    • Li X., et al. The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome. Cell 124 (2006) 381-392
    • (2006) Cell , vol.124 , pp. 381-392
    • Li, X.1
  • 28
    • 0242298321 scopus 로고    scopus 로고
    • Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein
    • Corn P.G., McDonald III E.R., Herman J.G., and El-Deiry W.S. Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein. Nat. Genet. 35 (2003) 229-237
    • (2003) Nat. Genet. , vol.35 , pp. 229-237
    • Corn, P.G.1    McDonald III, E.R.2    Herman, J.G.3    El-Deiry, W.S.4
  • 29
    • 85047691081 scopus 로고    scopus 로고
    • Heterozygous deficiency of hypoxia-inducible factor-2alpha protects mice against pulmonary hypertension and right ventricular dysfunction during prolonged hypoxia
    • Brusselmans K., Compernolle V., Tjwa M., Wiesener M.S., Maxwell P.H., Collen D., and Carmeliet P. Heterozygous deficiency of hypoxia-inducible factor-2alpha protects mice against pulmonary hypertension and right ventricular dysfunction during prolonged hypoxia. J. Clin. Invest. 111 (2003) 1519-1527
    • (2003) J. Clin. Invest. , vol.111 , pp. 1519-1527
    • Brusselmans, K.1    Compernolle, V.2    Tjwa, M.3    Wiesener, M.S.4    Maxwell, P.H.5    Collen, D.6    Carmeliet, P.7
  • 30
    • 0037134015 scopus 로고    scopus 로고
    • Recruitment of a 19S proteasome subcomplex to an activated promoter
    • Gonzalez F., Delahodde A., Kodadek T., and Johnston S.A. Recruitment of a 19S proteasome subcomplex to an activated promoter. Science 296 (2002) 548-550
    • (2002) Science , vol.296 , pp. 548-550
    • Gonzalez, F.1    Delahodde, A.2    Kodadek, T.3    Johnston, S.A.4
  • 31
    • 0037134022 scopus 로고    scopus 로고
    • Transcription. Proteasome parts at gene promoters
    • Ottosen S., Herrera F.J., and Triezenberg S.J. Transcription. Proteasome parts at gene promoters. Science 296 (2002) 479-481
    • (2002) Science , vol.296 , pp. 479-481
    • Ottosen, S.1    Herrera, F.J.2    Triezenberg, S.J.3
  • 32
    • 0010586475 scopus 로고    scopus 로고
    • The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair
    • Russell S.J., Reed S.H., Huang W., Friedberg E.C., and Johnston S.A. The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair. Mol. Cell. 3 (1999) 687-695
    • (1999) Mol. Cell. , vol.3 , pp. 687-695
    • Russell, S.J.1    Reed, S.H.2    Huang, W.3    Friedberg, E.C.4    Johnston, S.A.5
  • 33
    • 0035946294 scopus 로고    scopus 로고
    • HBV X protein targets HIV Tat-binding protein 1
    • Barak O., Aronheim A., and Shaul Y. HBV X protein targets HIV Tat-binding protein 1. Virology 283 (2001) 110-120
    • (2001) Virology , vol.283 , pp. 110-120
    • Barak, O.1    Aronheim, A.2    Shaul, Y.3
  • 34
    • 33846658069 scopus 로고    scopus 로고
    • The proteasome regulates HIV-1 transcription by both proteolytic and nonproteolytic mechanisms
    • Lassot I., et al. The proteasome regulates HIV-1 transcription by both proteolytic and nonproteolytic mechanisms. Mol. Cell 25 (2007) 369-383
    • (2007) Mol. Cell , vol.25 , pp. 369-383
    • Lassot, I.1
  • 35
    • 0033065326 scopus 로고    scopus 로고
    • Induction of the Tat-binding protein 1 gene accompanies the disabling of oncogenic erbB receptor tyrosine kinases
    • Park B.W., O'Rourke D.M., Wang Q., Davis J.G., Post A., Qian X., and Greene M.I. Induction of the Tat-binding protein 1 gene accompanies the disabling of oncogenic erbB receptor tyrosine kinases. Proc. Natl. Acad. Sci. USA 96 (1999) 6434-6438
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6434-6438
    • Park, B.W.1    O'Rourke, D.M.2    Wang, Q.3    Davis, J.G.4    Post, A.5    Qian, X.6    Greene, M.I.7
  • 36
    • 0034652143 scopus 로고    scopus 로고
    • Subcellular localization of proteasomes and their regulatory complexes in mammalian cells
    • Brooks P., et al. Subcellular localization of proteasomes and their regulatory complexes in mammalian cells. Biochem. J. 346 Pt 1 (2000) 155-161
    • (2000) Biochem. J. , vol.346 , Issue.PART 1 , pp. 155-161
    • Brooks, P.1
  • 37
    • 33845416970 scopus 로고    scopus 로고
    • Global organization and function of mammalian cytosolic proteasome pools: implications for PA28 and 19S regulatory complexes
    • Shibatani T., Carlson E.J., Larabee F., McCormack A.L., Fruh K., and Skach W.R. Global organization and function of mammalian cytosolic proteasome pools: implications for PA28 and 19S regulatory complexes. Mol. Biol. Cell 17 (2006) 4962-4971
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4962-4971
    • Shibatani, T.1    Carlson, E.J.2    Larabee, F.3    McCormack, A.L.4    Fruh, K.5    Skach, W.R.6
  • 38
    • 0035070697 scopus 로고    scopus 로고
    • Regulation of proteasome complexes by gamma-interferon and phosphorylation
    • Rivett A.J., Bose S., Brooks P., and Broadfoot K.I. Regulation of proteasome complexes by gamma-interferon and phosphorylation. Biochimie 83 (2001) 363-366
    • (2001) Biochimie , vol.83 , pp. 363-366
    • Rivett, A.J.1    Bose, S.2    Brooks, P.3    Broadfoot, K.I.4
  • 39
    • 17144389347 scopus 로고    scopus 로고
    • Growth factor regulation of a 26S proteasomal subunit in breast cancer
    • Barnes C.J., Li F., Talukder A.H., and Kumar R. Growth factor regulation of a 26S proteasomal subunit in breast cancer. Clin. Cancer Res. 11 (2005) 2868-2874
    • (2005) Clin. Cancer Res. , vol.11 , pp. 2868-2874
    • Barnes, C.J.1    Li, F.2    Talukder, A.H.3    Kumar, R.4
  • 41
    • 0032549704 scopus 로고    scopus 로고
    • The Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53
    • Pomerantz J., et al. The Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53. Cell 92 (1998) 713-723
    • (1998) Cell , vol.92 , pp. 713-723
    • Pomerantz, J.1
  • 42
    • 0032169516 scopus 로고    scopus 로고
    • The alternative product from the human CDKN2A locus, p14(ARF), participates in a regulatory feedback loop with p53 and MDM2
    • Stott F.J., et al. The alternative product from the human CDKN2A locus, p14(ARF), participates in a regulatory feedback loop with p53 and MDM2. EMBO J. 17 (1998) 5001-5014
    • (1998) EMBO J. , vol.17 , pp. 5001-5014
    • Stott, F.J.1
  • 43
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways
    • Zhang Y., Xiong Y., and Yarbrough W.G. ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways. Cell 92 (1998) 725-734
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3
  • 45
    • 24344433172 scopus 로고    scopus 로고
    • ARF directly binds DP1: interaction with DP1 coincides with the G1 arrest function of ARF
    • Datta A., et al. ARF directly binds DP1: interaction with DP1 coincides with the G1 arrest function of ARF. Mol. Cell. Biol. 25 (2005) 8024-8036
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8024-8036
    • Datta, A.1
  • 47
    • 4544240597 scopus 로고    scopus 로고
    • Inhibition of p63 transcriptional activity by p14ARF: functional and physical link between human ARF tumor suppressor and a member of the p53 family
    • Calabro V., Mansueto G., Santoro R., Gentilella A., Pollice A., Ghioni P., Guerrini L., and La Mantia G. Inhibition of p63 transcriptional activity by p14ARF: functional and physical link between human ARF tumor suppressor and a member of the p53 family. Mol. Cell. Biol. 24 (2004) 8529-8540
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8529-8540
    • Calabro, V.1    Mansueto, G.2    Santoro, R.3    Gentilella, A.4    Pollice, A.5    Ghioni, P.6    Guerrini, L.7    La Mantia, G.8
  • 48
    • 11144353897 scopus 로고    scopus 로고
    • Foxm1b transcription factor is essential for development of hepatocellular carcinomas and is negatively regulated by the p19ARF tumor suppressor
    • Kalinichenko V.V., et al. Foxm1b transcription factor is essential for development of hepatocellular carcinomas and is negatively regulated by the p19ARF tumor suppressor. Genes Dev. 18 (2004) 830-850
    • (2004) Genes Dev. , vol.18 , pp. 830-850
    • Kalinichenko, V.V.1
  • 51
    • 45549091465 scopus 로고    scopus 로고
    • Tumor suppressor ARF promotes non-classic proteasome-independent polyubiquitination of COMMD1
    • Huang Y., Wu M., and Li H.Y. Tumor suppressor ARF promotes non-classic proteasome-independent polyubiquitination of COMMD1. J. Biol. Chem. 283 (2008) 11453-11460
    • (2008) J. Biol. Chem. , vol.283 , pp. 11453-11460
    • Huang, Y.1    Wu, M.2    Li, H.Y.3
  • 52
    • 0035864758 scopus 로고    scopus 로고
    • Human ARF protein interacts with topoisomerase I and stimulates its activity
    • Karayan L., Riou J.F., Seite P., Migeon J., Cantereau A., and Larsen C.J. Human ARF protein interacts with topoisomerase I and stimulates its activity. Oncogene 20 (2001) 836-848
    • (2001) Oncogene , vol.20 , pp. 836-848
    • Karayan, L.1    Riou, J.F.2    Seite, P.3    Migeon, J.4    Cantereau, A.5    Larsen, C.J.6
  • 54
    • 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. ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 121 (2005) 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
  • 55
    • 25444505677 scopus 로고    scopus 로고
    • p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes the sumoylation of its binding partners
    • Rizos H., Woodruff S., and Kefford R.F. p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes the sumoylation of its binding partners. Cell Cycle 4 (2005) 597-603
    • (2005) Cell Cycle , vol.4 , pp. 597-603
    • Rizos, H.1    Woodruff, S.2    Kefford, R.F.3
  • 56
    • 33644758569 scopus 로고    scopus 로고
    • Targeting of C-terminal binding protein (CtBP) by ARF results in p53-independent apoptosis
    • Paliwal S., Pande S., Kovi R.C., Sharpless N.E., Bardeesy N., and Grossman S.R. Targeting of C-terminal binding protein (CtBP) by ARF results in p53-independent apoptosis. Mol. Cell. Biol. 26 (2006) 2360-2372
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2360-2372
    • Paliwal, S.1    Pande, S.2    Kovi, R.C.3    Sharpless, N.E.4    Bardeesy, N.5    Grossman, S.R.6
  • 57
    • 19644384513 scopus 로고    scopus 로고
    • Sumoylation induced by the Arf tumor suppressor: a p53-independent function
    • Tago K., Chiocca S., and Sherr C.J. Sumoylation induced by the Arf tumor suppressor: a p53-independent function. Proc. Natl. Acad. Sci. USA 102 (2005) 7689-7694
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7689-7694
    • Tago, K.1    Chiocca, S.2    Sherr, C.J.3
  • 59
    • 34547434064 scopus 로고    scopus 로고
    • Sumoylation of nucleophosmin/B23 regulates its subcellular localization, mediating cell proliferation and survival
    • Liu X., et al. Sumoylation of nucleophosmin/B23 regulates its subcellular localization, mediating cell proliferation and survival. Proc. Natl. Acad. Sci. USA 104 (2007) 9679-9684
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 9679-9684
    • Liu, X.1
  • 60
    • 0036892010 scopus 로고    scopus 로고
    • Differential regulation of E2F1, DP1, and the E2F1/DP1 complex by ARF
    • Datta A., Nag A., and Raychaudhuri P. Differential regulation of E2F1, DP1, and the E2F1/DP1 complex by ARF. Mol. Cell. Biol. 22 (2002) 8398-8408
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8398-8408
    • Datta, A.1    Nag, A.2    Raychaudhuri, P.3
  • 61
    • 0035836772 scopus 로고    scopus 로고
    • p19ARF targets certain E2F species for degradation
    • Martelli F., et al. p19ARF targets certain E2F species for degradation. Proc. Natl. Acad. Sci. USA 98 (2001) 4455-4460
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4455-4460
    • Martelli, F.1
  • 62
    • 34548239767 scopus 로고    scopus 로고
    • p14ARF regulates E2F-1 ubiquitination and degradation via a p53-dependent mechanism
    • Rizos H., Scurr L.L., Irvine M., Alling N.J., and Kefford R.F. p14ARF regulates E2F-1 ubiquitination and degradation via a p53-dependent mechanism. Cell Cycle 6 (2007) 1741-1747
    • (2007) Cell Cycle , vol.6 , pp. 1741-1747
    • Rizos, H.1    Scurr, L.L.2    Irvine, M.3    Alling, N.J.4    Kefford, R.F.5
  • 63
    • 1642499357 scopus 로고    scopus 로고
    • Physical and functional interactions of the Arf tumor suppressor protein with nucleophosmin/B23
    • Bertwistle D., Sugimoto M., and Sherr C.J. Physical and functional interactions of the Arf tumor suppressor protein with nucleophosmin/B23. Mol. Cell. Biol. 24 (2004) 985-996
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 985-996
    • Bertwistle, D.1    Sugimoto, M.2    Sherr, C.J.3
  • 64
    • 0345276485 scopus 로고    scopus 로고
    • Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation
    • Itahana K., Bhat K.P., Jin A., Itahana Y., Hawke D., Kobayashi R., and Zhang Y. Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation. Mol. Cell 12 (2003) 1151-1164
    • (2003) Mol. Cell , vol.12 , pp. 1151-1164
    • Itahana, K.1    Bhat, K.P.2    Jin, A.3    Itahana, Y.4    Hawke, D.5    Kobayashi, R.6    Zhang, Y.7
  • 65
    • 33745855088 scopus 로고    scopus 로고
    • Essential role of the B23/NPM core domain in regulating ARF binding and B23 stability
    • Enomoto T., Lindstrom M.S., Jin A., Ke H., and Zhang Y. Essential role of the B23/NPM core domain in regulating ARF binding and B23 stability. J. Biol. Chem. 281 (2006) 18463-18472
    • (2006) J. Biol. Chem. , vol.281 , pp. 18463-18472
    • Enomoto, T.1    Lindstrom, M.S.2    Jin, A.3    Ke, H.4    Zhang, Y.5
  • 66
    • 33645526300 scopus 로고    scopus 로고
    • Delocalization and destabilization of the Arf tumor suppressor by the leukemia-associated NPM mutant
    • Colombo E., et al. Delocalization and destabilization of the Arf tumor suppressor by the leukemia-associated NPM mutant. Cancer Res. 66 (2006) 3044-3050
    • (2006) Cancer Res. , vol.66 , pp. 3044-3050
    • Colombo, E.1
  • 67
    • 0142258245 scopus 로고    scopus 로고
    • Homeodomain interacting protein kinase 2 promotes apoptosis by downregulating the transcriptional corepressor CtBP
    • Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., and Goodman R.H. Homeodomain interacting protein kinase 2 promotes apoptosis by downregulating the transcriptional corepressor CtBP. Cell 115 (2003) 177-186
    • (2003) Cell , vol.115 , pp. 177-186
    • Zhang, Q.1    Yoshimatsu, Y.2    Hildebrand, J.3    Frisch, S.M.4    Goodman, R.H.5
  • 68
    • 0042195822 scopus 로고    scopus 로고
    • A non-proteolytic role for ubiquitin in Tat-mediated transactivation of the HIV-1 promoter
    • Bres V., et al. A non-proteolytic role for ubiquitin in Tat-mediated transactivation of the HIV-1 promoter. Nat. Cell Biol. 5 (2003) 754-761
    • (2003) Nat. Cell Biol. , vol.5 , pp. 754-761
    • Bres, V.1
  • 69
    • 20044386298 scopus 로고    scopus 로고
    • Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation
    • Lim K.L., et al. Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation. J. Neurosci. 25 (2005) 2002-2009
    • (2005) J. Neurosci. , vol.25 , pp. 2002-2009
    • Lim, K.L.1


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