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Volumn 365, Issue 2, 2008, Pages 232-238

The polyglutamine-expanded protein ataxin-3 decreases bcl-2 mRNA stability

Author keywords

Bcl 2; mRNA stability; Polyglutamine expanded ataxin 3; Spinocerebellar ataxia type 3

Indexed keywords

5,6 DICHLOROBENZIMIDAZOLE RIBOSIDE; ADENOSINE DERIVATIVE; ATAXIN 3; GREEN FLUORESCENT PROTEIN; MESSENGER RNA; POLYGLUTAMINE; PROTEIN BCL 2;

EID: 36248946819     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.10.162     Document Type: Article
Times cited : (11)

References (33)
  • 2
    • 0242693202 scopus 로고    scopus 로고
    • Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics
    • Scheel H., Tomiuk S., and Hofmann K. Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics. Hum. Mol. Genet. 12 (2003) 2845-2852
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2845-2852
    • Scheel, H.1    Tomiuk, S.2    Hofmann, K.3
  • 3
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett B., Li F., and Pittman R.N. The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum. Mol. Genet. 12 (2003) 3195-3205
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 4
    • 24744447434 scopus 로고    scopus 로고
    • Defining the role of ubiquitin-interacting motifs in the polyglutamine disease protein, ataxin-3
    • Berke S.J., Chai Y., Marrs G.L., Wen H., and Paulson H.L. Defining the role of ubiquitin-interacting motifs in the polyglutamine disease protein, ataxin-3. J. Biol. Chem. 280 (2005) 32026-32034
    • (2005) J. Biol. Chem. , vol.280 , pp. 32026-32034
    • Berke, S.J.1    Chai, Y.2    Marrs, G.L.3    Wen, H.4    Paulson, H.L.5
  • 5
    • 15444372240 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation
    • Burnett B.G., and Pittman R.N. The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation. Proc. Natl. Acad. Sci. USA 102 (2005) 4330-4335
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4330-4335
    • Burnett, B.G.1    Pittman, R.N.2
  • 8
    • 14344262672 scopus 로고    scopus 로고
    • Full-length expanded ataxin-3 enhances mitochondrial-mediated cell death and decreases Bcl-2 expression in human neuroblastoma cells
    • Tsai H.F., Tsai H.J., and Hsieh M. Full-length expanded ataxin-3 enhances mitochondrial-mediated cell death and decreases Bcl-2 expression in human neuroblastoma cells. Biochem. Biophys. Res. Commun. 324 (2004) 1274-1282
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 1274-1282
    • Tsai, H.F.1    Tsai, H.J.2    Hsieh, M.3
  • 9
    • 0037160106 scopus 로고    scopus 로고
    • Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities
    • Li F., Macfarian T., Pittman R.N., and Chakravarti D. Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities. J. Biol. Chem. 277 (2002) 45004-45012
    • (2002) J. Biol. Chem. , vol.277 , pp. 45004-45012
    • Li, F.1    Macfarian, T.2    Pittman, R.N.3    Chakravarti, D.4
  • 11
    • 33750962224 scopus 로고    scopus 로고
    • Ataxin-3 represses transcription via chromatin binding, interaction with histone deacetylase 3, and histone deacetylation
    • Evert B.O., Araujo J., Vieira-Saecker A.M., de Vos R.A., Harendza S., Klockgether T., and Wullner U. Ataxin-3 represses transcription via chromatin binding, interaction with histone deacetylase 3, and histone deacetylation. J. Neurosci. 26 (2006) 11474-11486
    • (2006) J. Neurosci. , vol.26 , pp. 11474-11486
    • Evert, B.O.1    Araujo, J.2    Vieira-Saecker, A.M.3    de Vos, R.A.4    Harendza, S.5    Klockgether, T.6    Wullner, U.7
  • 12
    • 0037494974 scopus 로고    scopus 로고
    • Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3
    • Wen F.C., Li Y.H., Tsai H.F., Lin C.H., Li C., Liu C.S., Lii C.K., Nukina N., and Hsieh M. Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3. FEBS Lett. 546 (2003) 307-314
    • (2003) FEBS Lett. , vol.546 , pp. 307-314
    • Wen, F.C.1    Li, Y.H.2    Tsai, H.F.3    Lin, C.H.4    Li, C.5    Liu, C.S.6    Lii, C.K.7    Nukina, N.8    Hsieh, M.9
  • 16
    • 0034571171 scopus 로고    scopus 로고
    • Huntington's disease: the challenge for cell biologists
    • Tobin A.J., and Signer E.R. Huntington's disease: the challenge for cell biologists. Trends Cell Biol. 10 (2000) 531-536
    • (2000) Trends Cell Biol. , vol.10 , pp. 531-536
    • Tobin, A.J.1    Signer, E.R.2
  • 17
    • 33746117919 scopus 로고    scopus 로고
    • Polyglutamine disease: recent advances in the neuropathology of dentatorubral-pallidoluysian atrophy
    • Yamada M., Shimohata M., Sato T., Tsuji S., and Takahashi H. Polyglutamine disease: recent advances in the neuropathology of dentatorubral-pallidoluysian atrophy. Neuropathology 26 (2006) 346-351
    • (2006) Neuropathology , vol.26 , pp. 346-351
    • Yamada, M.1    Shimohata, M.2    Sato, T.3    Tsuji, S.4    Takahashi, H.5
  • 18
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., and Reed J.C. Mitochondria and apoptosis. Science 281 (1998) 1309-1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 19
    • 0026454763 scopus 로고
    • Prevention of programmed cell death of sympathetic neurons by the bcl-2 proto-oncogene
    • Garcia I., Martinou I., Tsujimoto Y., and Martinou J.C. Prevention of programmed cell death of sympathetic neurons by the bcl-2 proto-oncogene. Science 258 (1992) 302-304
    • (1992) Science , vol.258 , pp. 302-304
    • Garcia, I.1    Martinou, I.2    Tsujimoto, Y.3    Martinou, J.C.4
  • 22
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai Z.N., Milliman C.L., and Korsmeyer S.J. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74 (1993) 609-619
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 23
    • 0033562535 scopus 로고    scopus 로고
    • Activation of the bcl-2 promoter by nerve growth factor is mediated by the p42/p44 MAPK cascade
    • Liu Y.Z., Boxer L.M., and Latchman D.S. Activation of the bcl-2 promoter by nerve growth factor is mediated by the p42/p44 MAPK cascade. Nucleic Acids Res. 27 (1999) 2086-2090
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2086-2090
    • Liu, Y.Z.1    Boxer, L.M.2    Latchman, D.S.3
  • 24
    • 0032479443 scopus 로고    scopus 로고
    • Bcl-2 transcription from the proximal p2 promoter is activated in neuronal cells by Brn-3a POU family transcription factor
    • Smith M.D., Ensor E.A., Coffin R.S., Boxer L.M., and Latchman D.S. Bcl-2 transcription from the proximal p2 promoter is activated in neuronal cells by Brn-3a POU family transcription factor. J. Biol. Chem. 273 (1998) 16715-16722
    • (1998) J. Biol. Chem. , vol.273 , pp. 16715-16722
    • Smith, M.D.1    Ensor, E.A.2    Coffin, R.S.3    Boxer, L.M.4    Latchman, D.S.5
  • 25
    • 0024561487 scopus 로고
    • 5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole inhibits transcription elongation by RNA polymerase II in vitro
    • Chodosh L.A., Fire A., Samuels M., and Sharp P.A. 5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole inhibits transcription elongation by RNA polymerase II in vitro. J. Biol. Chem. 264 (1989) 2250-2257
    • (1989) J. Biol. Chem. , vol.264 , pp. 2250-2257
    • Chodosh, L.A.1    Fire, A.2    Samuels, M.3    Sharp, P.A.4
  • 26
    • 0029973094 scopus 로고    scopus 로고
    • Interrelationships of the pathways of mRNA decay and translation in eukaryotic cells
    • Jacobson A., and Peltz S.W. Interrelationships of the pathways of mRNA decay and translation in eukaryotic cells. Annu. Rev. Biochem. 65 (1996) 693-739
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 693-739
    • Jacobson, A.1    Peltz, S.W.2
  • 27
    • 1642442715 scopus 로고    scopus 로고
    • Identification of nucleolin as an AU-rich element binding protein involved in bcl-2 mRNA stabilization
    • Sengupta T.K., Bandyopadhyay S., Fernandes D.J., and Spicer E.K. Identification of nucleolin as an AU-rich element binding protein involved in bcl-2 mRNA stabilization. J. Biol. Chem. 12 (2004) 10855-10863
    • (2004) J. Biol. Chem. , vol.12 , pp. 10855-10863
    • Sengupta, T.K.1    Bandyopadhyay, S.2    Fernandes, D.J.3    Spicer, E.K.4
  • 29
    • 0033026714 scopus 로고    scopus 로고
    • Mechanisms of apoptosis avoidance in cancer
    • Reed J.C. Mechanisms of apoptosis avoidance in cancer. Curr. Opin. Oncol. 11 (1999) 68-75
    • (1999) Curr. Opin. Oncol. , vol.11 , pp. 68-75
    • Reed, J.C.1
  • 30
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat. Med. 3 (1997) 614-620
    • (1997) Nat. Med. , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 31
    • 0033971901 scopus 로고    scopus 로고
    • Bcl-2 family: life-or-death switch
    • Tsujimoto Y., and Shimizu S. Bcl-2 family: life-or-death switch. FEBS Lett. 466 (2000) 6-10
    • (2000) FEBS Lett. , vol.466 , pp. 6-10
    • Tsujimoto, Y.1    Shimizu, S.2
  • 32
    • 0029884448 scopus 로고    scopus 로고
    • Down regulation of Bcl-2 is the first step on Fas-mediated apoptosis of male reproductive tract
    • Suzuki A., Matsuzawa A., and Iguchi T. Down regulation of Bcl-2 is the first step on Fas-mediated apoptosis of male reproductive tract. Oncogene 13 (1996) 31-37
    • (1996) Oncogene , vol.13 , pp. 31-37
    • Suzuki, A.1    Matsuzawa, A.2    Iguchi, T.3
  • 33
    • 0034055242 scopus 로고    scopus 로고
    • Cell cycle arrest enhances the in vitro cellular toxicity of the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch
    • Yoshizawa T., Yamagishi Y., Koseki N., Goto J., Yoshida H., Shibasaki F., Shoji S., and Kanazawa I. Cell cycle arrest enhances the in vitro cellular toxicity of the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch. Hum. Mol. Genet. 9 (2000) 69-78
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 69-78
    • Yoshizawa, T.1    Yamagishi, Y.2    Koseki, N.3    Goto, J.4    Yoshida, H.5    Shibasaki, F.6    Shoji, S.7    Kanazawa, I.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.