메뉴 건너뛰기




Volumn 25, Issue 7, 2006, Pages 1547-1558

An arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis

(19)  Boeddrich, Annett a   Gaumer, Sébastien b,h   Haacke, Annette c   Tzvetkov, Nikolay c   Albrecht, Mario d   Evert, Bernd O e   Müller, Eva C a   Lurz, Rudi f   Breuer, Peter c   Schugardt, Nancy a   Plaßmann, Stephanie a   Xu, Kexiang b   Warrick, John M b   Suopanki, Jaana a   Wüllner, Ullrich e   Frank, Ronald g   Hartl, Ulrich F c   Bonini, Nancy M b   Wanker, Erich E a  


Author keywords

Ataxin 3; Polyglutamine aggregation; VCP

Indexed keywords

ARGININE; ATAXIN 3; CHAPERONE; LYSINE; MUTANT PROTEIN; PROTEIN P97;

EID: 33645735557     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601043     Document Type: Article
Times cited : (138)

References (43)
  • 1
    • 3242890363 scopus 로고    scopus 로고
    • Structural and functional analysis of ataxin-2 and ataxin-3
    • Albrecht M, Golatta M, Wullner U, Lengauer T (2004) Structural and functional analysis of ataxin-2 and ataxin-3. Eur J Biochem 271: 3155-3170
    • (2004) Eur J Biochem , vol.271 , pp. 3155-3170
    • Albrecht, M.1    Golatta, M.2    Wullner, U.3    Lengauer, T.4
  • 2
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils
    • Bevivino AE, Loll PJ (2001) An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils. Proc Natl Acad Sci USA 98: 11955-11960
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 3
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett B, Li F, Pittman RN (2003) The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum Mol Genet 12: 3195-3205
    • (2003) Hum Mol Genet , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 4
    • 0033030565 scopus 로고    scopus 로고
    • Evidence for proteasome involvement in polyglutamine disease: Localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro
    • Chai Y, Koppenhafer SL, Shoesmith SJ, Perez MK, Paulson HL (1999) Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum Mol Genet 8: 573-682
    • (1999) Hum Mol Genet , vol.8 , pp. 573-682
    • Chai, Y.1    Koppenhafer, S.L.2    Shoesmith, S.J.3    Perez, M.K.4    Paulson, H.L.5
  • 5
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi +]
    • Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW (1995) Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi +]. Science 268: 880-884
    • (1995) Science , vol.268 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 6
    • 0141507032 scopus 로고    scopus 로고
    • Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
    • DeLaBarre B, Brunger AT (2003) Complete structure of p97/valosin- containing protein reveals communication between nucleotide domains. Nat Struct Biol 10: 856-863
    • (2003) Nat Struct Biol , vol.10 , pp. 856-863
    • DeLaBarre, B.1    Brunger, A.T.2
  • 7
    • 14644415865 scopus 로고    scopus 로고
    • Nucleotide dependent motion and mechanism of action of p97/VCP
    • DeLaBarre B, Brunger AT (2005) Nucleotide dependent motion and mechanism of action of p97/VCP. J Mol Biol 347: 437-452
    • (2005) J Mol Biol , vol.347 , pp. 437-452
    • DeLaBarre, B.1    Brunger, A.T.2
  • 9
    • 1842576796 scopus 로고    scopus 로고
    • Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47
    • Dreveny I, Kondo H, Uchiyama K, Shaw A, Zhang X, Freemont PS (2004a) Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47. EMBO J 23: 1030-1039
    • (2004) EMBO J , vol.23 , pp. 1030-1039
    • Dreveny, I.1    Kondo, H.2    Uchiyama, K.3    Shaw, A.4    Zhang, X.5    Freemont, P.S.6
  • 12
    • 0026656122 scopus 로고
    • Spot-Synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on a membrane support
    • Frank R (1992) Spot-Synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support. Tetrahedron 48: 9217-9232
    • (1992) Tetrahedron , vol.48 , pp. 9217-9232
    • Frank, R.1
  • 13
    • 0030329981 scopus 로고    scopus 로고
    • SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes
    • Frank R, Overwin H (1996) SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes. Methods Mol Biol 66: 149-169
    • (1996) Methods Mol Biol , vol.66 , pp. 149-169
    • Frank, R.1    Overwin, H.2
  • 20
    • 2542468586 scopus 로고    scopus 로고
    • Can flies help humans treat neurodegenerative diseases?
    • Marsh JL, Thompson LM (2004) Can flies help humans treat neurodegenerative diseases? BioEssays 26: 485-496
    • (2004) BioEssays , vol.26 , pp. 485-496
    • Marsh, J.L.1    Thompson, L.M.2
  • 21
    • 0041563693 scopus 로고    scopus 로고
    • Domain architecture of the polyglutamine protein ataxin-3: A globular domain followed by a flexible tail
    • Masino L, Musi V, Menon RP, Fusi P, Kelly G, Frenkiel TA, Trottier Y, Pastore A (2003) Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail. FEBS Lett 549: 21-25
    • (2003) FEBS Lett , vol.549 , pp. 21-25
    • Masino, L.1    Musi, V.2    Menon, R.P.3    Fusi, P.4    Kelly, G.5    Frenkiel, T.A.6    Trottier, Y.7    Pastore, A.8
  • 22
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G (2000) A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J 19: 2181-2192
    • (2000) EMBO J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 23
    • 0037986563 scopus 로고    scopus 로고
    • Vacuole-creating protein in neurodegenerative diseases in humans
    • Mizuno Y, Hori S, Kakizuka A, Okamoto K (2003) Vacuole-creating protein in neurodegenerative diseases in humans. Neurosci Lett 343: 77-80
    • (2003) Neurosci Lett , vol.343 , pp. 77-80
    • Mizuno, Y.1    Hori, S.2    Kakizuka, A.3    Okamoto, K.4
  • 25
    • 0027981247 scopus 로고
    • Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes
    • Parsell DA, Kowal AS, Lindquist S (1994) Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J Biol Chem 269: 4480-4487
    • (1994) J Biol Chem , vol.269 , pp. 4480-4487
    • Parsell, D.A.1    Kowal, A.S.2    Lindquist, S.3
  • 26
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaper-one
    • Rape M, Hoppe T, Gorr I, Kalocay M, Richly H, Jentsch S (2001) Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaper-one. Cell 107: 667-677
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 29
    • 0034160086 scopus 로고    scopus 로고
    • Protein-only inheritance in yeast: Something to get [PSI +]-ched about
    • Serio TR, Lindquist SL (2000) Protein-only inheritance in yeast: something to get [PSI +]-ched about. Trends Cell Biol 10: 98-105
    • (2000) Trends Cell Biol , vol.10 , pp. 98-105
    • Serio, T.R.1    Lindquist, S.L.2
  • 30
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter J, Lindquist S (2004) Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304: 1793-1797
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 31
    • 0037024380 scopus 로고    scopus 로고
    • Cdc48 can distinguish between native and non-native proteins in the absence of cofactors
    • Thoms S (2002) Cdc48 can distinguish between native and non-native proteins in the absence of cofactors. FEBS Lett 520: 107-110
    • (2002) FEBS Lett , vol.520 , pp. 107-110
    • Thoms, S.1
  • 32
    • 0033867992 scopus 로고    scopus 로고
    • Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B
    • Wang G, Sawai N, Kotliarova S, Kanazawa I, Nukina N (2000) Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B. Hum Mol Genet 9: 1795-1803
    • (2000) Hum Mol Genet , vol.9 , pp. 1795-1803
    • Wang, G.1    Sawai, N.2    Kotliarova, S.3    Kanazawa, I.4    Nukina, N.5
  • 33
    • 0037427531 scopus 로고    scopus 로고
    • Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities
    • Wang Q, Song C, Li CC (2003) Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities. Biochem Biophys Res Commun 300: 253-260
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 253-260
    • Wang, Q.1    Song, C.2    Li, C.C.3
  • 34
    • 1642309633 scopus 로고    scopus 로고
    • Molecular perspectives on p97-VCP: Progress in understanding its structure and diverse biological functions
    • Wang Q, Song C, Li CC (2004) Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions. J Struct Biol 146: 44-57
    • (2004) J Struct Biol , vol.146 , pp. 44-57
    • Wang, Q.1    Song, C.2    Li, C.C.3
  • 35
    • 0032879437 scopus 로고    scopus 로고
    • Membrane filter assay for detection of amyloid-like polyglutamine- containing protein aggregates
    • Wanker EE, Scherzinger E, Heiser V, Sittler A, Eickhoff H, Lehrach H (1999) Membrane filter assay for detection of amyloid-like polyglutamine- containing protein aggregates. Methods Enzymol 309: 375-386
    • (1999) Methods Enzymol , vol.309 , pp. 375-386
    • Wanker, E.E.1    Scherzinger, E.2    Heiser, V.3    Sittler, A.4    Eickhoff, H.5    Lehrach, H.6
  • 36
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick JM, Chan HY, Gray-Board GL, Chai Y, Paulson HL, Bonini NM (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 23: 425-428
    • (1999) Nat Genet , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 38
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts GD, Wymer J, Kovach MJ, Mehta SG, Mumm S, Darvish D, Pestronk A, Whyte MP, Kimonis VE (2004) Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet 36: 377-381
    • (2004) Nat Genet , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3    Mehta, S.G.4    Mumm, S.5    Darvish, D.6    Pestronk, A.7    Whyte, M.P.8    Kimonis, V.E.9
  • 39
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y, Meyer HH, Rapoport TA (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162: 71-84
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 41
    • 0033855808 scopus 로고    scopus 로고
    • VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells
    • Zhang H, Wang Q, Kajino K, Greene MI (2000a) VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells. DNA Cell Biol 19: 253-263
    • (2000) DNA Cell Biol , vol.19 , pp. 253-263
    • Zhang, H.1    Wang, Q.2    Kajino, K.3    Greene, M.I.4
  • 43
    • 8544263881 scopus 로고    scopus 로고
    • AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation
    • Zhong X, Shen Y, Ballar P, Apostolou A, Agami R, Fang S (2004) AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation. J Biol Chem 279: 45676-45684
    • (2004) J Biol Chem , vol.279 , pp. 45676-45684
    • Zhong, X.1    Shen, Y.2    Ballar, P.3    Apostolou, A.4    Agami, R.5    Fang, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.