메뉴 건너뛰기




Volumn 13, Issue 3, 2011, Pages 273-281

The Machado-Joseph disease deubiquitylase ATX-3 couples longevity and proteostasis

Author keywords

[No Author keywords available]

Indexed keywords

ATAXIN 3; INSULIN; PROTEIN P97; SOMATOMEDIN C;

EID: 79952280797     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb2200     Document Type: Article
Times cited : (77)

References (53)
  • 2
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • DOI 10.1002/(SICI)1521-1878(200005)22:5<442::AID-BIES6>3.0.CO;2-Q
    • Ciechanover, A., Orian, A. & Schwartz, A. L. Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays 22, 442-451 (2000). (Pubitemid 30308270)
    • (2000) BioEssays , vol.22 , Issue.5 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 3
    • 77749319656 scopus 로고    scopus 로고
    • A cellular perspective on conformational disease: The role of genetic background and proteostasis networks
    • Gidalevitz, T., Kikis, E. A. & Morimoto, R. I. A cellular perspective on conformational disease: the role of genetic background and proteostasis networks. Curr. Opin. Struct. Biol. 20, 23-32 (2010).
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 23-32
    • Gidalevitz, T.1    Kikis, E.A.2    Morimoto, R.I.3
  • 4
  • 5
    • 34548624245 scopus 로고    scopus 로고
    • Aging and regulated protein degradation: Who has the UPPer hand?
    • DOI 10.1111/j.1474-9726.2007.00329.x
    • Vernace, V. A., Schmidt-Glenewinkel, T. & Figueiredo-Pereira, M. E. Aging and regulated protein degradation: who has the UPPer hand? Aging Cell 6, 599-606 (2007). (Pubitemid 47400042)
    • (2007) Aging Cell , vol.6 , Issue.5 , pp. 599-606
    • Vernace, V.A.1    Schmidt-Glenewinkel, T.2    Figueiredo-Pereira, M.E.3
  • 6
    • 59449095881 scopus 로고    scopus 로고
    • Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process
    • Tonoki, A. et al. Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process. Mol. Cell Biol. 29, 1095-1106 (2009).
    • (2009) Mol. Cell Biol. , vol.29 , pp. 1095-1106
    • Tonoki, A.1
  • 9
    • 67651004289 scopus 로고    scopus 로고
    • A conserved ubiquitination pathway determines longevity in response to diet restriction
    • Carrano, A. C., Liu, Z., Dillin, A. & Hunter, T. A conserved ubiquitination pathway determines longevity in response to diet restriction. Nature 460, 396-399 (2009).
    • (2009) Nature , vol.460 , pp. 396-399
    • Carrano, A.C.1    Liu, Z.2    Dillin, A.3    Hunter, T.4
  • 10
    • 66349098677 scopus 로고    scopus 로고
    • Proteasomal regulation of the hypoxic response modulates aging in C. elegans
    • Mehta, R. et al. Proteasomal regulation of the hypoxic response modulates aging in C. elegans. Science 324, 1196-1198 (2009).
    • (2009) Science , vol.324 , pp. 1196-1198
    • Mehta, R.1
  • 11
    • 33846596646 scopus 로고    scopus 로고
    • RLE-1, an E3 Ubiquitin Ligase, Regulates C. elegans Aging by Catalyzing DAF-16 Polyubiquitination
    • DOI 10.1016/j.devcel.2006.12.002, PII S1534580706005600
    • Li, W., Gao, B., Lee, S. M., Bennett, K. & Fang, D. RLE-1, an E3 ubiquitin ligase, regulates C. elegans aging by catalyzing DAF-16 polyubiquitination. Dev. Cell 12, 235-246 (2007). (Pubitemid 46172901)
    • (2007) Developmental Cell , vol.12 , Issue.2 , pp. 235-246
    • Li, W.1    Gao, B.2    Lee, S.-M.3    Bennett, K.4    Fang, D.5
  • 12
    • 66349105688 scopus 로고    scopus 로고
    • The WD40 repeat protein WDR-23 functions with the CUL4/DDB1 ubiquitin ligase to regulate nuclear abundance and activity of SKN-1 in Caenorhabditis elegans
    • Choe, K. P., Przybysz, A. J. & Strange, K. The WD40 repeat protein WDR-23 functions with the CUL4/DDB1 ubiquitin ligase to regulate nuclear abundance and activity of SKN-1 in Caenorhabditis elegans. Mol. Cell Biol. 29, 2704-2715 (2009).
    • (2009) Mol. Cell Biol. , vol.29 , pp. 2704-2715
    • Choe, K.P.1    Przybysz, A.J.2    Strange, K.3
  • 13
    • 67149107430 scopus 로고    scopus 로고
    • HIF-1 modulates dietary restriction-mediated lifespan extension via IRE-1 in Caenorhabditis elegans
    • Chen, D., Thomas, E. L. & Kapahi, P. HIF-1 modulates dietary restriction-mediated lifespan extension via IRE-1 in Caenorhabditis elegans. PLoS Genet. 5, e1000486 (2009).
    • (2009) PLoS Genet. , vol.5
    • Chen, D.1    Thomas, E.L.2    Kapahi, P.3
  • 14
    • 33845939821 scopus 로고    scopus 로고
    • Cdc48 (p97): A "molecular gearbox" in the ubiquitin pathway?
    • Jentsch, S. & Rumpf, S. Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway? Trends Biochem. Sci. 32, 6-11 (2007).
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 6-11
    • Jentsch, S.1    Rumpf, S.2
  • 15
    • 33749258342 scopus 로고    scopus 로고
    • A conserved role of Caenorhabditis elegans CDC-48 in ER-associated protein degradation
    • DOI 10.1016/j.jsb.2006.02.015, PII S1047847706000700, AAA + Proteins
    • Mouysset, J., Kaehler, C. & Hoppe, T. A conserved role of Caenorhabditis elegans CDC-48 in ER-associated protein degradation. J. Struct. Biol. 156, 41-49 (2006). (Pubitemid 44486057)
    • (2006) Journal of Structural Biology , vol.156 , Issue.1 , pp. 41-49
    • Mouysset, J.1    Kahler, C.2    Hoppe, T.3
  • 17
    • 16244373679 scopus 로고    scopus 로고
    • Multiubiquitylation by E4 enzymes: 'One size' doesn't fit all
    • DOI 10.1016/j.tibs.2005.02.004
    • Hoppe, T. Multiubiquitylation by E4 enzymes: 'one size' doesn't fit all. Trends Biochem. Sci. 30, 183-187 (2005). (Pubitemid 40463307)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.4 , pp. 183-187
    • Hoppe, T.1
  • 18
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P. & Harper, J. W. Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403 (2009).
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 19
    • 55549086868 scopus 로고    scopus 로고
    • The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains
    • Winborn, B. J. et al. The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains. J. Biol. Chem. 283, 26436-26443 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 26436-26443
    • Winborn, B.J.1
  • 20
    • 60549100850 scopus 로고    scopus 로고
    • Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3
    • Todi, S. V. et al. Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3. EMBO J. 28, 372-382 (2009).
    • (2009) EMBO J. , vol.28 , pp. 372-382
    • Todi, S.V.1
  • 22
    • 33748988214 scopus 로고    scopus 로고
    • Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3
    • DOI 10.1083/jcb.200605100
    • Wang, Q., Li, L. & Ye, Y. Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3. J. Cell Biol. 174, 963-971 (2006). (Pubitemid 44455185)
    • (2006) Journal of Cell Biology , vol.174 , Issue.7 , pp. 963-971
    • Wang, Q.1    Li, A.2    Ye, Y.3
  • 23
    • 33645735557 scopus 로고    scopus 로고
    • An arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis
    • Boeddrich, A. et al. An arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis. EMBO J. 25, 1547-1558 (2006).
    • (2006) EMBO J. , vol.25 , pp. 1547-1558
    • Boeddrich, A.1
  • 24
    • 67650457634 scopus 로고    scopus 로고
    • ATX-3, CDC-48 and UBXN-5: A new trimolecular complex in Caenorhabditis elegans
    • Rodrigues, A. J. et al. ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans. Biochem. Biophys. Res. Commun. 386, 575-581 (2009).
    • (2009) Biochem. Biophys. Res. Commun. , vol.386 , pp. 575-581
    • Rodrigues, A.J.1
  • 26
    • 4043096960 scopus 로고    scopus 로고
    • Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans
    • DOI 10.1016/j.cell.2004.07.014, PII S0092867404007032
    • Hoppe, T. et al. Regulation of the myosin-directed chaperone UNC-45 by a novel E3/ E4-multiubiquitylation complex in C. elegans. Cell 118, 337-349 (2004). (Pubitemid 39061114)
    • (2004) Cell , vol.118 , Issue.3 , pp. 337-349
    • Hoppe, T.1    Cassata, G.2    Barral, J.M.3    Springer, W.4    Hutagalung, A.H.5    Epstein, H.F.6    Baumeister, R.7
  • 27
    • 51349137580 scopus 로고    scopus 로고
    • Cell cycle progression requires the CDC-48UFD-1/NPL-4 complex for efficient DNA replication
    • Mouysset, J. et al. Cell cycle progression requires the CDC-48UFD-1/NPL-4 complex for efficient DNA replication. Proc. Natl Acad. Sci. USA 105, 12879-12884 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 12879-12884
    • Mouysset, J.1
  • 28
    • 33646845471 scopus 로고    scopus 로고
    • Comparative analysis of expression of two p97 homologues in Caenorhabditis elegans
    • DOI 10.1016/j.bbrc.2006.04.160, PII S0006291X06009715
    • Yamauchi, S., Yamanaka, K. & Ogura, T. Comparative analysis of expression of two p97 homologues in Caenorhabditis elegans. Biochem. Biophys. Res. Commun. 345, 746-753 (2006). (Pubitemid 43776994)
    • (2006) Biochemical and Biophysical Research Communications , vol.345 , Issue.2 , pp. 746-753
    • Yamauchi, S.1    Yamanaka, K.2    Ogura, T.3
  • 30
    • 0030813398 scopus 로고    scopus 로고
    • Daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans
    • DOI 10.1126/science.277.5328.942
    • Kimura, K. D., Tissenbaum, H. A., Liu, Y. & Ruvkun, G. daf?2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans. Science 277, 942-946 (1997). (Pubitemid 27366677)
    • (1997) Science , vol.277 , Issue.5328 , pp. 942-946
    • Kimura, K.D.1    Tissenbaum, H.A.2    Liu, Y.3    Ruvkun, G.4
  • 31
    • 0034967720 scopus 로고    scopus 로고
    • Regulation of the Caenorhabditis elegans longevity protein DAF-16 by insulin/IGF-1 and germline signaling
    • DOI 10.1038/88850
    • Lin, K., Hsin, H., Libina, N. & Kenyon, C. Regulation of the Caenorhabditis elegans longevity protein DAF-16 by insulin/IGF-1 and germline signaling. Nat. Genet. 28, 139-145 (2001). (Pubitemid 32538058)
    • (2001) Nature Genetics , vol.28 , Issue.2 , pp. 139-145
    • Lin, K.1    Hsin, H.2    Libina, N.3    Kenyon, C.4
  • 32
    • 0030659557 scopus 로고    scopus 로고
    • The fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans
    • DOI 10.1038/40194
    • Ogg, S. et al. The Fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans. Nature 389, 994-999 (1997). (Pubitemid 27485694)
    • (1997) Nature , vol.389 , Issue.6654 , pp. 994-999
    • Ogg, S.1    Paradis, S.2    Gottlieb, S.3    Patterson, G.I.4    Lee, L.5    Tissenbaum, H.A.6    Ruvkun, G.7
  • 33
    • 34249888736 scopus 로고    scopus 로고
    • PHA-4/Foxa mediates diet-restriction-induced longevity of C. elegans
    • DOI 10.1038/nature05837, PII NATURE05837
    • Panowski, S. H., Wolff, S., Aguilaniu, H., Durieux, J. & Dillin, A. PHA-4/Foxa mediates diet-restriction-induced longevity of C. elegans. Nature 447, 550-555 (2007). (Pubitemid 46868041)
    • (2007) Nature , vol.447 , Issue.7144 , pp. 550-555
    • Panowski, S.H.1    Wolff, S.2    Aguilaniu, H.3    Durieux, J.4    Dillin, A.5
  • 34
    • 34249891333 scopus 로고    scopus 로고
    • Two neurons mediate diet-restriction-induced longevity in C. elegans
    • DOI 10.1038/nature05904, PII NATURE05904
    • Bishop, N. A. & Guarente, L. Two neurons mediate diet-restriction- induced longevity in C. elegans. Nature 447, 545-549 (2007). (Pubitemid 46868049)
    • (2007) Nature , vol.447 , Issue.7144 , pp. 545-549
    • Bishop, N.A.1    Guarente, L.2
  • 35
    • 0037466652 scopus 로고    scopus 로고
    • DAF-16 target genes that control C. elegans Life-span and metabolism
    • DOI 10.1126/science.1083614
    • Lee, S. S., Kennedy, S., Tolonen, A. C. & Ruvkun, G. DAF-16 target genes that control C. elegans life-span and metabolism. Science 300, 644-647 (2003). (Pubitemid 36520589)
    • (2003) Science , vol.300 , Issue.5619 , pp. 644-647
    • Lee, S.S.1    Kennedy, S.2    Tolonen, A.C.3    Ruvkun, G.4
  • 36
    • 33744976074 scopus 로고    scopus 로고
    • C. elegans SIR-2.1 Interacts with 14-3-3 Proteins to Activate DAF-16 and Extend Life Span
    • DOI 10.1016/j.cell.2006.04.036, PII S0092867406006180
    • Berdichevsky, A., Viswanathan, M., Horvitz, H. R. & Guarente, L. C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span. Cell 125, 1165-1177 (2006). (Pubitemid 43866202)
    • (2006) Cell , vol.125 , Issue.6 , pp. 1165-1177
    • Berdichevsky, A.1    Viswanathan, M.2    Horvitz, H.R.3    Guarente, L.4
  • 37
    • 0033576579 scopus 로고    scopus 로고
    • Regulation of lifespan by sensory perception in Caenorhabditis elegans
    • Apfeld, J. & Kenyon, C. Regulation of lifespan by sensory perception in Caenorhabditis elegans. Nature 402, 804-809 (1999).
    • (1999) Nature , vol.402 , pp. 804-809
    • Apfeld, J.1    Kenyon, C.2
  • 38
    • 77953091249 scopus 로고    scopus 로고
    • Insulin/IGF-1 signaling mutants reprogram ER stress response regulators to promote longevity
    • Henis-Korenblit, S. et al. Insulin/IGF-1 signaling mutants reprogram ER stress response regulators to promote longevity. Proc. Natl Acad. Sci. USA 107, 9730-9735 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 9730-9735
    • Henis-Korenblit, S.1
  • 40
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E. S., Ma, P. C., Ota, I. M. & Varshavsky, A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442-17456 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 41
    • 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 (2000). (Pubitemid 30313959)
    • (2000) Nature Biotechnology , vol.18 , Issue.5 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 42
    • 48249084602 scopus 로고    scopus 로고
    • E1 ubiquitin-activating enzyme UBA-1 plays multiple roles throughout C. elegans development
    • Kulkarni, M. & Smith, H. E. E1 ubiquitin-activating enzyme UBA-1 plays multiple roles throughout C. elegans development. PLoS Genet. 4, e1000131 (2008).
    • (2008) PLoS Genet. , vol.4
    • Kulkarni, M.1    Smith, H.E.2
  • 43
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander, D. The emerging complexity of protein ubiquitination. Biochem. Soc. Trans. 37, 937-953 (2009).
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 937-953
    • Komander, D.1
  • 44
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl, M. et al. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644 (1999). (Pubitemid 29122806)
    • (1999) Cell , vol.96 , Issue.5 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 45
    • 3042719644 scopus 로고    scopus 로고
    • Definitive evidence for Ufd2-catalyzed elongation of the ubiquitin chain through Lys48 linkage
    • DOI 10.1016/j.bbrc.2004.05.216, PII S0006291X04012665
    • Saeki, Y., Tayama, Y., Toh-e, A. & Yokosawa, H. Definitive evidence for Ufd2-catalyzed elongation of the ubiquitin chain through Lys48 linkage. Biochem. Biophys. Res. Commun. 320, 840-845 (2004). (Pubitemid 38887219)
    • (2004) Biochemical and Biophysical Research Communications , vol.320 , Issue.3 , pp. 840-845
    • Saeki, Y.1    Tayama, Y.2    Toh-e, A.3    Yokosawa, H.4
  • 46
    • 49549117842 scopus 로고    scopus 로고
    • Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies
    • Newton, K. et al. Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies. Cell 134, 668-678 (2008).
    • (2008) Cell , vol.134 , pp. 668-678
    • Newton, K.1
  • 47
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • DOI 10.1016/j.cell.2004.11.013, PII S0092867404010864
    • Richly, H. et al. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120, 73-84 (2005). (Pubitemid 40094604)
    • (2005) Cell , vol.120 , Issue.1 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 48
    • 72149114101 scopus 로고    scopus 로고
    • Together Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor
    • Zhang, D. et al. Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor. Mol. Cell 36, 1018-1033 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 1018-1033
    • Zhang, D.1
  • 49
    • 67650427174 scopus 로고    scopus 로고
    • S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains
    • Kim, H. T., Kim, K. P., Uchiki, T., Gygi, S. P. & Goldberg, A. L. S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains. EMBO J. 28, 1867-1877 (2009).
    • (2009) EMBO J. , vol.28 , pp. 1867-1877
    • Kim, H.T.1    Kim, K.P.2    Uchiki, T.3    Gygi, S.P.4    Goldberg, A.L.5
  • 50
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. The genetics of Caenorhabditis elegans. Genetics 77, 71-94 (1974).
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 52
    • 0035099902 scopus 로고    scopus 로고
    • Creation of low-copy integrated transgenic lines in Caenorhabditis elegans
    • Praitis, V., Casey, E., Collar, D. & Austin, J. Creation of low-copy integrated transgenic lines in Caenorhabditis elegans. Genetics 157, 1217-1226 (2001). (Pubitemid 32225014)
    • (2001) Genetics , vol.157 , Issue.3 , pp. 1217-1226
    • Praitis, V.1    Casey, E.2    Collar, D.3    Austin, J.4
  • 53
    • 0032578911 scopus 로고    scopus 로고
    • Specific interference by ingested dsRNA
    • Timmons, L. & Fire, A. Specific interference by ingested dsRNA. Nature 395, 854 (1998).
    • (1998) Nature , vol.395 , pp. 854
    • Timmons, L.1    Fire, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.