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Volumn , Issue 69, 2012, Pages

Monitoring of ubiquitin-proteasome activity in living cells using a degron (dgn)-destabilized green fluorescent protein (GFP)-based reporter protein

Author keywords

Biomedical engineering; Cellular biology; Flow cytometry; GFP; GFP dgn; GFP dgnFS; Human diploid fibroblasts; Issue 69; Lentiviral particles; Medicine; Molecular biology; Plasmid; Proteasome activity; Vector; Virology

Indexed keywords


EID: 84869238255     PISSN: 1940087X     EISSN: None     Source Type: Journal    
DOI: 10.3791/3327     Document Type: Article
Times cited : (10)

References (18)
  • 1
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • doi:10.1146/annurev.bi.65.070196.004101 (1996)
    • Coux, O., Tanaka, K., & Goldberg, A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847, doi:10.1146/annurev.bi.65.070196.004101 (1996).
    • Annu. Rev. Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 2
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • [pii] S0300-9084(01)01250-0
    • Davies, K.J. Degradation of oxidized proteins by the 20S proteasome. Biochimi. 83, 301-310, [pii] S0300-9084(01)01250-0 (2001).
    • (2001) Biochimi , vol.83 , pp. 301-310
    • Davies, K.J.1
  • 3
    • 72949084163 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and endothelial (dys)function
    • [pii] cvp315 doi:10.1093/cvr/cvp315
    • Stangl, K. & Stangl, V. The ubiquitin-proteasome pathway and endothelial (dys)function. Cardiovasc. Res. 85, 281-290, [pii] cvp315 doi:10.1093/cvr/cvp315 (2009).
    • (2009) Cardiovasc. Res , vol.85 , pp. 281-290
    • Stangl, K.1    Stangl, V.2
  • 4
    • 77955729735 scopus 로고    scopus 로고
    • Roles of the ubiquitin-proteosome system in neurogenesis
    • [pii] 12551 doi:10.4161/cc.9.16.12551
    • Tuoc, T.C. & Stoykova, A. Roles of the ubiquitin-proteosome system in neurogenesis. Cell Cycle. 9, 3174-3180, [pii] 12551 doi:10.4161/cc.9.16.12551 (2010).
    • (2010) Cell Cycle , vol.9 , pp. 3174-3180
    • Tuoc, T.C.1    Stoykova, A.2
  • 5
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • [pii] S0092-8674(94)90462-6
    • Rock, K.L., et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78, 761-771, [pii] S0092-8674(94)90462-6 (1994).
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1
  • 6
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • [pii] 10.1007/s00401-009-0560-x
    • Lehman, N.L. The ubiquitin proteasome system in neuropathology. Acta Neuropathol. 118, 329-347, [pii] 10.1007/s00401-009-0560-x (2009).
    • (2009) Acta Neuropathol , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 7
    • 79951511983 scopus 로고    scopus 로고
    • Functional Interplay between mitochondrial and proteasome activity in skin aging
    • [pii] jid2010383 doi: 10.1038/jid.2010.383
    • Koziel, R., Greussing, R., Maier, A.B., Declercq, L., & Jansen-Durr, P. Functional Interplay between mitochondrial and proteasome activity in skin aging. J. Invest. Dermatol. 131, 594-603, [pii] jid2010383 doi: 10.1038/jid.2010.383 (2010).
    • (2010) J. Invest. Dermatol , vol.131 , pp. 594-603
    • Koziel, R.1    Greussing, R.2    Maier, A.B.3    Declercq, L.4    Jansen-Durr, P.5
  • 8
    • 78049404330 scopus 로고    scopus 로고
    • Post-translational modification of cellular proteins by ubiquitin and ubiquitin-like molecules: Role in cellular senescence and aging
    • Grillari, J., Grillari-Voglauer, R., & Jansen-Durr, P. Post-translational modification of cellular proteins by ubiquitin and ubiquitin-like molecules: role in cellular senescence and aging. Adv. Exp. Med. Biol. 694, 172-196 (2010).
    • (2010) Adv. Exp. Med. Biol , vol.694 , pp. 172-196
    • Grillari, J.1    Grillari-Voglauer, R.2    Jansen-Durr, P.3
  • 9
    • 0037082124 scopus 로고    scopus 로고
    • Age-dependent declines in proteasome activity in the heart
    • doi:10.1006/abbi.2001.2663S0003986101926633
    • Bulteau, A.L., Szweda, L.I., & Friguet, B. Age-dependent declines in proteasome activity in the heart. Arch. Biochem. Biophys. 397, 298-304, doi:10.1006/abbi.2001.2663S0003986101926633 (2002).
    • Arch. Biochem. Biophys , vol.397 , pp. 298-304
    • Bulteau, A.L.1    Szweda, L.I.2    Friguet, B.3
  • 10
    • 77049107294 scopus 로고    scopus 로고
    • Proteasomal activity in skeletal muscle: A matter of assay design, muscle type, and age
    • pii] S0003-2697(09)00873-2 doi:10.1016/j.ab.2009.12.026
    • Strucksberg, K.H., Tangavelou, K., Schroder, R., & Clemen, C.S. Proteasomal activity in skeletal muscle: A matter of assay design, muscle type, and age. Anal. Biochem. [pii] S0003-2697(09)00873-2 doi:10.1016/j.ab.2009.12.026 (2009).
    • (2009) Anal. Biochem
    • Strucksberg, K.H.1    Tangavelou, K.2    Schroder, R.3    Clemen, C.S.4
  • 11
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N.F., Sampat, R.M., & Kopito, R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 292, 1552-1555 (2001).
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 12
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • doi:10.1038/75406
    • Dantuma, N.P., Lindsten, K., Glas, R., Jellne, M., & Masucci, M.G. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells. Nat. Biotechnol. 18, 538-543, doi:10.1038/75406 (2000).
    • (2000) Nat. Biotechnol , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 13
    • 0043208904 scopus 로고    scopus 로고
    • A transgenic mouse model of the ubiquitin/proteasome system
    • doi:10.1038/nbt851nbt851
    • Lindsten, K., Menendez-Benito, V., Masucci, M.G., & Dantuma, N.P. A transgenic mouse model of the ubiquitin/proteasome system. Nat. Biotechnol. 21, 897-902, doi:10.1038/nbt851nbt851 (2003).
    • (2003) Nat. Biotechnol , vol.21 , pp. 897-902
    • Lindsten, K.1    Menendez-Benito, V.2    Masucci, M.G.3    Dantuma, N.P.4
  • 14
    • 33644883329 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts
    • [pii] 05-4869fje doi:10.1096/fj.05-4869fje
    • Liu, J., et al. Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts. FASEB J. 20, 362-364, [pii] 05-4869fje doi:10.1096/fj.05-4869fje (2006).
    • (2006) FASEB J , vol.20 , pp. 362-364
    • Liu, J.1
  • 15
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • [pii] ddi064 doi:10.1093/hmg/ddi064
    • Bowman, A.B., Yoo, S.Y., Dantuma, N.P., & Zoghbi, H.Y. Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum. Mol. Genet. 14, 679-691, [pii] ddi064 doi:10.1093/hmg/ddi064 (2005).
    • (2005) Hum. Mol. Genet , vol.14 , pp. 679-691
    • Bowman, A.B.1    Yoo, S.Y.2    Dantuma, N.P.3    Zoghbi, H.Y.4
  • 16
    • 0035099055 scopus 로고    scopus 로고
    • Lack of proteasome active site allostery as revealed by subunit-specific inhibitors
    • [pii] S1097-2765(01)00188-5
    • Myung, J., Kim, K.B., Lindsten, K., Dantuma, N.P., & Crews, C.M. Lack of proteasome active site allostery as revealed by subunit-specific inhibitors. Mol. Cell. 7, 411-420, [pii] S1097-2765(01)00188-5 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 411-420
    • Myung, J.1    Kim, K.B.2    Lindsten, K.3    Dantuma, N.P.4    Crews, C.M.5
  • 17
    • 28844485595 scopus 로고    scopus 로고
    • Monitoring of ubiquitin-dependent proteolysis with green fluorescent protein substrates
    • [pii]S0076-6879(05)99034-4 doi:10.1016/S0076-6879(05)99034-4
    • Menendez-Benito, V., Heessen, S., & Dantuma, N.P. Monitoring of ubiquitin-dependent proteolysis with green fluorescent protein substrates. Methods Enzymol. 399, 490-511, [pii]S0076-6879(05)99034-4 doi:10.1016/S0076-6879(05)99034-4 (2005).
    • (2005) Methods Enzymol , vol.399 , pp. 490-511
    • Menendez-Benito, V.1    Heessen, S.2    Dantuma, N.P.3
  • 18
    • 70350098392 scopus 로고    scopus 로고
    • The NADPH oxidase Nox4 restricts the replicative lifespan of human endothelial cells
    • [pii] BJ20090666 doi:10.1042/BJ20090666
    • Lener, B., et al. The NADPH oxidase Nox4 restricts the replicative lifespan of human endothelial cells. Biochem. J. 423, 363-374, [pii] BJ20090666 doi:10.1042/BJ20090666 (2009).
    • (2009) Biochem. J , vol.423 , pp. 363-374
    • Lener, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.