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Volumn 67, Issue 12, 2010, Pages 2025-2038

Tubulin chaperone e binds microtubules and proteasomes and protects against misfolded protein stress

Author keywords

CAP Gly; Pac2; Proteasome; Rpn1; Rpn10; TBCE; Ubiquitin like domain

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN; CHAPERONE; F BOX PROTEIN; FUNGAL PROTEIN; GLYCINE; PROTEASOME; PROTEIN PAC2; S PHASE KINASE ASSOCIATED PROTEIN; S PHASE KINASE ASSOCIATED PROTEIN 1; TUBULIN; TUBULIN CHAPERONE E; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 77953024195     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-010-0308-8     Document Type: Article
Times cited : (19)

References (61)
  • 2
    • 0030748745 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability
    • 9215891 1:CAS:528:DyaK2sXmsVartLk%3D
    • MA Hoyt JP Macke BT Roberts JR Geiser 1997 Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability Genetics 146 849 857 9215891 1:CAS:528:DyaK2sXmsVartLk%3D
    • (1997) Genetics , vol.146 , pp. 849-857
    • Hoyt, M.A.1    MacKe, J.P.2    Roberts, B.T.3    Geiser, J.R.4
  • 3
    • 0032824097 scopus 로고    scopus 로고
    • Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast
    • 10473641 1:CAS:528:DyaK1MXmtFektrk%3D
    • PA Radcliffe D Hirata L Vardy T Toda 1999 Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast Mol Biol Cell 10 2987 3001 10473641 1:CAS:528:DyaK1MXmtFektrk%3D
    • (1999) Mol Biol Cell , vol.10 , pp. 2987-3001
    • Radcliffe, P.A.1    Hirata, D.2    Vardy, L.3    Toda, T.4
  • 4
    • 0030820735 scopus 로고    scopus 로고
    • Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
    • DOI 10.1083/jcb.138.4.821
    • G Tian SA Lewis B Feierbach T Stearns H Rommelaere C Ampe NJ Cowan 1997 Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors J Cell Biol 138 821 832 10.1083/jcb.138.4.821 9265649 1:CAS:528:DyaK2sXlsleiurw%3D (Pubitemid 27365045)
    • (1997) Journal of Cell Biology , vol.138 , Issue.4 , pp. 821-832
    • Tian, G.1    Lewis, S.A.2    Feierbach, B.3    Stearns, T.4    Rommelaere, H.5    Ampe, C.6    Cowan, N.J.7
  • 5
    • 0033545205 scopus 로고    scopus 로고
    • Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with α-tubulin
    • DOI 10.1083/jcb.144.1.113
    • B Feierbach E Nogales KH Downing T Stearns 1999 Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin J Cell Biol 144 113 124 10.1083/jcb.144.1.113 9885248 1:CAS:528:DyaK1MXjs1yhtw%3D%3D (Pubitemid 29047015)
    • (1999) Journal of Cell Biology , vol.144 , Issue.1 , pp. 113-124
    • Feierbach, B.1    Nogales, E.2    Downing, K.H.3    Stearns, T.4
  • 6
    • 0035715785 scopus 로고    scopus 로고
    • Type II chaperonins, prefoldin, and the tubulin-specific chaperones
    • DOI 10.1016/S0065-3233(01)59003-8
    • NJ Cowan SA Lewis 2001 Type II chaperonins, prefoldin, and the tubulin-specific chaperones Adv Protein Chem 59 73 104 10.1016/S0065-3233(01) 59003-8 11868281 1:STN:280:DC%2BD387jtlehug%3D%3D (Pubitemid 34169302)
    • (2001) Advances in Protein Chemistry , vol.59 , pp. 73-104
    • Cowan, N.J.1    Lewis, S.A.2
  • 7
    • 18744404214 scopus 로고    scopus 로고
    • Review: Postchaperonin tubulin folding cofactors and their role in microtubule dynamics
    • 10.1006/jsbi.2001.4386 11580271 1:CAS:528:DC%2BD3MXntFKqurs%3D
    • M Lopez-Fanarraga J Avila A Guasch M Coll JC Zabala 2001 Review: postchaperonin tubulin folding cofactors and their role in microtubule dynamics J Struct Biol 135 219 229 10.1006/jsbi.2001.4386 11580271 1:CAS:528: DC%2BD3MXntFKqurs%3D
    • (2001) J Struct Biol , vol.135 , pp. 219-229
    • Lopez-Fanarraga, M.1    Avila, J.2    Guasch, A.3    Coll, M.4    Zabala, J.C.5
  • 8
    • 0037175395 scopus 로고    scopus 로고
    • Missense mutation in the tubulin-specific chaperone e (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease
    • 10.1083/jcb.200208001 12446740 1:CAS:528:DC%2BD38XptVyqtLs%3D
    • H Bommel G Xie W Rossoll S Wiese S Jablonka T Boehm M Sendtner 2002 Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease J Cell Biol 159 563 569 10.1083/jcb.200208001 12446740 1:CAS:528: DC%2BD38XptVyqtLs%3D
    • (2002) J Cell Biol , vol.159 , pp. 563-569
    • Bommel, H.1    Xie, G.2    Rossoll, W.3    Wiese, S.4    Jablonka, S.5    Boehm, T.6    Sendtner, M.7
  • 9
    • 0036842251 scopus 로고    scopus 로고
    • A missense mutation in Tbce causes progressive motor neuronopathy in mice
    • DOI 10.1038/ng1016
    • N Martin J Jaubert P Gounon E Salido G Haase M Szatanik JL Guenet 2002 A missense mutation in Tbce causes progressive motor neuronopathy in mice Nat Genet 32 443 447 10.1038/ng1016 12389029 1:CAS:528:DC%2BD38Xot1Kls7g%3D (Pubitemid 35266123)
    • (2002) Nature Genetics , vol.32 , Issue.3 , pp. 443-447
    • Martin, N.1    Jaubert, J.2    Gounon, P.3    Salido, E.4    Haase, G.5    Szatanik, M.6    Guenet, J.-L.7
  • 10
    • 0027535154 scopus 로고
    • Sequence homologies between four cytoskeleton-associated proteins
    • DOI 10.1016/0968-0004(93)90159-K
    • K Riehemann C Sorg 1993 Sequence homologies between four cytoskeleton-associated proteins Trends Biochem Sci 18 82 83 10.1016/0968-0004(93)90159-K 8480366 1:CAS:528:DyaK3sXkt1ejtrc%3D (Pubitemid 23080697)
    • (1993) Trends in Biochemical Sciences , vol.18 , Issue.3 , pp. 82-83
    • Riehemann, K.1    Sorg, C.2
  • 11
    • 2942610866 scopus 로고    scopus 로고
    • Domain analysis of the tubulin cofactor system: A model for tubulin folding and dimerization
    • DOI 10.1186/1471-2105-4-46
    • M Grynberg L Jaroszewski A Godzik 2003 Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization BMC Bioinformatics 4 46 53 10.1186/1471-2105-4-46 14536023 (Pubitemid 38751224)
    • (2003) BMC Bioinformatics , vol.4 , pp. 46
    • Grynberg, M.1    Jaroszewski, L.2    Godzik, A.3
  • 13
    • 33644747344 scopus 로고    scopus 로고
    • A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules
    • DOI 10.1038/ncb1370, PII N1370
    • TL Culver-Hanlon SA Lex AD Stephens NJ Quintyne SJ King 2006 A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules Nat Cell Biol 8 264 270 10.1038/ncb1370 16474384 1:CAS:528:DC%2BD28XhvVKhtLo%3D (Pubitemid 43336068)
    • (2006) Nature Cell Biology , vol.8 , Issue.3 , pp. 264-270
    • Culver-Hanlon, T.L.1    Lex, S.A.2    Stephens, A.D.3    Quintyne, N.J.4    King, S.J.5
  • 14
    • 0029929297 scopus 로고    scopus 로고
    • CLIPs for organelle-microtubule interactions
    • DOI 10.1016/0962-8924(96)10017-9
    • JE Rickard TE Kreis 1996 CLIPs for organelle-microtubule interactions Trends Cell Biol 6 178 183 10.1016/0962-8924(96)10017-9 15157469 1:CAS:528:DyaK28Xjtlent7s%3D (Pubitemid 26127381)
    • (1996) Trends in Cell Biology , vol.6 , Issue.5 , pp. 178-183
    • Rickard, J.E.1    Kreis, T.E.2
  • 15
    • 27844560722 scopus 로고    scopus 로고
    • Gigaxonin interacts with tubulin folding cofactor B and controls its degradation through the ubiquitin-proteasome pathway
    • DOI 10.1016/j.cub.2005.10.052, PII S0960982205013059
    • W Wang J Ding E Allen P Zhu L Zhang H Vogel Y Yang 2005 Gigaxonin interacts with tubulin folding cofactor B and controls its degradation through the ubiquitin-proteasome pathway Curr Biol 15 2050 2055 10.1016/j.cub.2005.10. 052 16303566 1:CAS:528:DC%2BD2MXht1GnsrrN (Pubitemid 41654630)
    • (2005) Current Biology , vol.15 , Issue.22 , pp. 2050-2055
    • Wang, W.1    Ding, J.2    Allen, E.3    Zhu, P.4    Zhang, L.5    Vogel, H.6    Yang, Y.7
  • 16
    • 8744267531 scopus 로고    scopus 로고
    • Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B
    • DOI 10.1074/jbc.M409422200
    • BL Lytle FC Peterson SH Qiu M Luo Q Zhao JL Markley BF Volkman 2004 Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B J Biol Chem 279 46787 46793 10.1074/jbc.M409422200 15364906 1:CAS:528: DC%2BD2cXptFaqu7s%3D (Pubitemid 39518328)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 46787-46793
    • Lytle, B.L.1    Peterson, F.C.2    Qiu, S.-H.3    Luo, M.4    Zhao, Q.5    Markley, J.L.6    Volkman, B.F.7
  • 18
    • 33846669353 scopus 로고    scopus 로고
    • Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer dissociation
    • DOI 10.1016/j.yexcr.2006.09.002, PII S0014482706003673
    • D Kortazar ML Fanarraga G Carranza J Bellido JC Villegas J Avila JC Zabala 2007 Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer dissociation Exp Cell Res 313 425 436 10.1016/j.yexcr.2006.09.002 17184771 1:CAS:528:DC%2BD2sXhtlakur4%3D (Pubitemid 46188632)
    • (2007) Experimental Cell Research , vol.313 , Issue.3 , pp. 425-436
    • Kortazar, D.1    Fanarraga, M.L.2    Carranza, G.3    Bellido, J.4    Villegas, J.C.5    Avila, J.6    Zabala, J.C.7
  • 19
    • 20444384416 scopus 로고    scopus 로고
    • Proteasome plasticity
    • DOI 10.1016/j.febslet.2005.04.048, PII S0014579305005235
    • MH Glickman D Raveh 2005 Proteasome plasticity FEBS Lett 579 3214 3223 10.1016/j.febslet.2005.04.048 15890341 1:CAS:528:DC%2BD2MXltFSqurw%3D (Pubitemid 40804666)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3214-3223
    • Glickman, M.H.1    Raveh, D.2
  • 20
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • DOI 10.1038/nrm1336
    • CM Pickart RE Cohen 2004 Proteasomes and their kin: proteases in the machine age Nat Rev Mol Cell Biol 5 177 187 10.1038/nrm1336 14990998 1:CAS:528:DC%2BD2cXhs1CltLw%3D (Pubitemid 38325799)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.3 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 21
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • DOI 10.1126/science.1075898
    • R Verma L Aravind R Oania WH McDonald JR Yates 3rd EV Koonin RJ Deshaies 2002 Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome Science 298 611 615 10.1126/science.1075898 12183636 1:CAS:528:DC%2BD38XotVWisL0%3D (Pubitemid 35215317)
    • (2002) Science , vol.298 , Issue.5593 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates III, J.R.5    Koonin, E.V.6    Deshaies, R.J.7
  • 22
    • 0347087494 scopus 로고    scopus 로고
    • Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome
    • DOI 10.1074/jbc.M307050200
    • A Guterman MH Glickman 2004 Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome J Biol Chem 279 1729 1738 10.1074/jbc.M307050200 14581483 1:CAS:528:DC%2BD2cXisF2ntg%3D%3D (Pubitemid 38084440)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 1729-1738
    • Guterman, A.1    Glickman, M.H.2
  • 24
    • 4544290828 scopus 로고    scopus 로고
    • Protein degradation: Recognition of ubiquitinylated substrates
    • DOI 10.1016/j.cub.2004.09.012, PII S0960982204006888
    • R Hartmann-Petersen C Gordon 2004 Protein degradation: recognition of ubiquitinylated substrates Curr Biol 14 R754 R756 10.1016/j.cub.2004.09.012 15380085 1:CAS:528:DC%2BD2cXnvFans7s%3D (Pubitemid 39239346)
    • (2004) Current Biology , vol.14 , Issue.18
    • Hartmann-Petersen, R.1    Gordon, C.2
  • 25
    • 23144449583 scopus 로고    scopus 로고
    • Delivery of ubiquitinated substrates to protein-unfolding machines
    • DOI 10.1038/ncb0805-742
    • S Elsasser D Finley 2005 Delivery of ubiquitinated substrates to protein-unfolding machines Nat Cell Biol 7 742 749 10.1038/ncb0805-742 16056265 1:CAS:528:DC%2BD2MXmvVCltLc%3D (Pubitemid 41079042)
    • (2005) Nature Cell Biology , vol.7 , Issue.8 , pp. 742-749
    • Elsasser, S.1    Finley, D.2
  • 26
    • 20444417275 scopus 로고    scopus 로고
    • The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease
    • DOI 10.1128/MCB.25.13.5355-5362.2005
    • L Kaplun R Tzirkin A Bakhrat N Shabek Y Ivantsiv D Raveh 2005 The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease Mol Cell Biol 25 5355 5362 10.1128/MCB.25.13.5355-5362.2005 15964793 1:CAS:528:DC%2BD2MXlslCjsLc%3D (Pubitemid 40853573)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.13 , pp. 5355-5362
    • Kaplun, L.1    Tzirkin, R.2    Bakhrat, A.3    Shabek, N.4    Ivantsiv, Y.5    Raveh, D.6
  • 27
    • 33644513063 scopus 로고    scopus 로고
    • Turnover of SCFUfo1 complexes requires the UbL-UbA motif protein, Ddi1
    • 10.1128/MCB.26.5.1579-1588.2006 16478980 1:CAS:528:DC%2BD28XitlGntb4%3D
    • Y Ivantsiv L Kaplun R Tzirkin-Goldin N Shabek D Raveh 2006 Turnover of SCFUfo1 complexes requires the UbL-UbA motif protein, Ddi1 Mol Cell Biol 26 1579 1588 10.1128/MCB.26.5.1579-1588.2006 16478980 1:CAS:528:DC%2BD28XitlGntb4%3D
    • (2006) Mol Cell Biol , vol.26 , pp. 1579-1588
    • Ivantsiv, Y.1    Kaplun, L.2    Tzirkin-Goldin, R.3    Shabek, N.4    Raveh, D.5
  • 28
    • 40849113190 scopus 로고    scopus 로고
    • Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins
    • DOI 10.1186/1471-2091-9-4
    • AM Goh KJ Walters S Elsasser R Verma RJ Deshaies D Finley PM Howley 2008 Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins BMC Biochem 9 4 10.1186/1471-2091-9-4 18234089 1:CAS:528:DC%2BD1cXisFKiurs%3D (Pubitemid 351393244)
    • (2008) BMC Biochemistry , vol.9 , Issue.1 , pp. 4
    • Goh, A.M.1    Walters, K.J.2    Elsasser, S.3    Verma, R.4    Deshaies, R.J.5    Finley, D.6    Howley, P.M.7
  • 30
    • 33751581527 scopus 로고    scopus 로고
    • Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway
    • DOI 10.1038/sj.emboj.7601418, PII 7601418
    • T Ishii M Funakoshi H Kobayashi 2006 Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway EMBO J 25 5492 5503 10.1038/sj.emboj.7601418 17082762 1:CAS:528:DC%2BD28Xht1Cnt7jE (Pubitemid 44847190)
    • (2006) EMBO Journal , vol.25 , Issue.23 , pp. 5492-5503
    • Ishii, T.1    Funakoshi, M.2    Kobayashi, H.3
  • 31
    • 55049090325 scopus 로고    scopus 로고
    • Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome
    • 10.1016/j.molcel.2008.10.011 18995839 1:CAS:528:DC%2BD1cXhsVSms7%2FL
    • Y Matiuhin DS Kirkpatrick I Ziv W Kim A Dakshinamurthy O Kleifeld SP Gygi N Reis MH Glickman 2008 Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome Mol Cell 32 415 425 10.1016/j.molcel.2008.10.011 18995839 1:CAS:528:DC%2BD1cXhsVSms7%2FL
    • (2008) Mol Cell , vol.32 , pp. 415-425
    • Matiuhin, Y.1    Kirkpatrick, D.S.2    Ziv, I.3    Kim, W.4    Dakshinamurthy, A.5    Kleifeld, O.6    Gygi, S.P.7    Reis, N.8    Glickman, M.H.9
  • 32
    • 0036295955 scopus 로고    scopus 로고
    • Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis
    • DOI 10.1016/S0006-291X(02)00340-6, PII S0006291X02003406
    • Y Saeki A Saitoh A Toh-e H Yokosawa 2002 Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis Biochem Biophys Res Commun 293 986 992 10.1016/S0006-291X(02)00340-6 12051757 1:CAS:528:DC%2BD38XktlGrur0%3D (Pubitemid 34694139)
    • (2002) Biochemical and Biophysical Research Communications , vol.293 , Issue.3 , pp. 986-992
    • Saeki, Y.1    Saitoh, A.2    Toh-e, A.3    Yokosawa, H.4
  • 33
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • 11029046 1:CAS:528:DC%2BD3cXnslWnt7g%3D
    • R Verma S Chen R Feldman D Schieltz J Yates J Dohmen RJ Deshaies 2000 Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes Mol Biol Cell 11 3425 3439 11029046 1:CAS:528:DC%2BD3cXnslWnt7g%3D
    • (2000) Mol Biol Cell , vol.11 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7
  • 34
    • 43149093941 scopus 로고    scopus 로고
    • A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates
    • 10.1074/jbc.M705893200 18174173 1:CAS:528:DC%2BD1cXivFyjuro%3D
    • C Lipson G Alalouf M Bajorek E Rabinovich A Atir-Lande M Glickman S Bar-Nun 2008 A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates J Biol Chem 283 7166 7175 10.1074/jbc.M705893200 18174173 1:CAS:528:DC%2BD1cXivFyjuro%3D
    • (2008) J Biol Chem , vol.283 , pp. 7166-7175
    • Lipson, C.1    Alalouf, G.2    Bajorek, M.3    Rabinovich, E.4    Atir-Lande, A.5    Glickman, M.6    Bar-Nun, S.7
  • 35
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • DOI 10.1016/j.cell.2004.06.014, PII S0092867404005835
    • R Verma R Oania J Graumann RJ Deshaies 2004 Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system Cell 118 99 110 10.1016/j.cell.2004.06.014 15242647 1:CAS:528: DC%2BD2cXlvFejtbk%3D (Pubitemid 38902817)
    • (2004) Cell , vol.118 , Issue.1 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 36
    • 0142184341 scopus 로고    scopus 로고
    • Global analysis of protein localization in budding yeast
    • DOI 10.1038/nature02026
    • WK Huh JV Falvo LC Gerke AS Carroll RW Howson JS Weissman EK O'Shea 2003 Global analysis of protein localization in budding yeast Nature 425 686 691 10.1038/nature02026 14562095 1:CAS:528:DC%2BD3sXotV2iu7g%3D (Pubitemid 37314307)
    • (2003) Nature , vol.425 , Issue.6959 , pp. 686-691
    • Huh, W.-K.1    Falvo, J.V.2    Gerke, L.C.3    Carroll, A.S.4    Howson, R.W.5    Weissman, J.S.6    O'Shea, E.K.7
  • 37
    • 0031774336 scopus 로고    scopus 로고
    • Cse1p is involved in export of yeast importin alpha from the nucleus
    • 9774694 1:CAS:528:DyaK1cXmvF2nsb8%3D
    • J Solsbacher P Maurer FR Bischoff G Schlenstedt 1998 Cse1p is involved in export of yeast importin alpha from the nucleus Mol Cell Biol 18 6805 6815 9774694 1:CAS:528:DyaK1cXmvF2nsb8%3D
    • (1998) Mol Cell Biol , vol.18 , pp. 6805-6815
    • Solsbacher, J.1    Maurer, P.2    Bischoff, F.R.3    Schlenstedt, G.4
  • 39
    • 1542467522 scopus 로고    scopus 로고
    • DNA damage response-mediated degradation of Ho endonuclease via the ubiquitin system involves its nuclear export
    • DOI 10.1074/jbc.M308671200
    • L Kaplun Y Ivantsiv A Bakhrat D Raveh 2003 DNA damage response-mediated degradation of Ho endonuclease via the ubiquitin system involves its nuclear export J Biol Chem 278 48727 48734 10.1074/jbc.M308671200 14506225 1:CAS:528:DC%2BD3sXptlGktLY%3D (Pubitemid 41079514)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.49 , pp. 48727-48734
    • Kaplun, L.1    Ivantsiv, Y.2    Bakhrat, A.3    Raveh, D.4
  • 41
    • 0033953565 scopus 로고    scopus 로고
    • Nob1p, a new essential protein, associates with the 26S proteasome of growing Saccharomyces cerevisiae cells
    • DOI 10.1016/S0378-1119(99)00566-1, PII S0378111999005661
    • Y Tone N Tanahashi K Tanaka M Fujimuro H Yokosawa A Toh-e 2000 Nob1p, a new essential protein, associates with the 26S proteasome of growing saccharomyces cerevisiae cells Gene 243 37 45 10.1016/S0378-1119(99)00566-1 10675611 1:CAS:528:DC%2BD3cXhsFCmsL0%3D (Pubitemid 30079703)
    • (2000) Gene , vol.243 , Issue.1-2 , pp. 37-45
    • Tone, Y.1    Tanahashi, N.2    Tanaka, K.3    Fujimuro, M.4    Yokosawa, H.5    Toh-e, A.6
  • 42
    • 0028363764 scopus 로고
    • Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization
    • 8206959 1:CAS:528:DyaK2cXksFarsbo%3D
    • TG Huang DD Hackney 1994 Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization J Biol Chem 269 16493 16501 8206959 1:CAS:528:DyaK2cXksFarsbo%3D
    • (1994) J Biol Chem , vol.269 , pp. 16493-16501
    • Huang, T.G.1    Hackney, D.D.2
  • 43
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • DOI 10.1016/S0962-8924(98)01346-4
    • DH Lee AL Goldberg 1998 Proteasome inhibitors: valuable new tools for cell biologists Trends Cell Biol 8 397 403 10.1016/S0962-8924(98)01346-4 9789328 1:CAS:528:DyaK1cXmvFWjtbc%3D (Pubitemid 28458705)
    • (1998) Trends in Cell Biology , vol.8 , Issue.10 , pp. 397-403
    • Lee, D.H.1
  • 44
    • 33947539481 scopus 로고    scopus 로고
    • Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue
    • DOI 10.1038/ncb1558, PII NCB1558
    • T Ravid M Hochstrasser 2007 Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue Nat Cell Biol 9 422 427 10.1038/ncb1558 17310239 1:CAS:528:DC%2BD2sXjs12jsr4%3D (Pubitemid 46511075)
    • (2007) Nature Cell Biology , vol.9 , Issue.4 , pp. 422-427
    • Ravid, T.1    Hochstrasser, M.2
  • 45
    • 0033596977 scopus 로고    scopus 로고
    • 1 cyclin ubiquitination with complexes containing SCF(Grr1) and Rbx1
    • DOI 10.1126/science.284.5414.662
    • D Skowyra DM Koepp T Kamura MN Conrad RC Conaway JW Conaway SJ Elledge JW Harper 1999 Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1 Science 284 662 665 10.1126/science.284.5414.662 10213692 1:CAS:528:DyaK1MXislyrurw%3D (Pubitemid 29289594)
    • (1999) Science , vol.284 , Issue.5414 , pp. 662-665
    • Skowyra, D.1    Koepp, D.M.2    Kamura, T.3    Conrad, M.N.4    Conaway, R.C.5    Conaway, J.W.6    Elledge, S.J.7    Harper, J.W.8
  • 46
    • 67649202108 scopus 로고    scopus 로고
    • Drosophila Tubulin-specific chaperone e functions at neuromuscular synapses and is required for microtubule network formation
    • 10.1242/dev.029983 19297412 1:CAS:528:DC%2BD1MXntFaks74%3D
    • S Jin L Pan Z Liu Q Wang Z Xu YQ Zhang 2009 Drosophila Tubulin-specific chaperone E functions at neuromuscular synapses and is required for microtubule network formation Development 136 1571 1581 10.1242/dev.029983 19297412 1:CAS:528:DC%2BD1MXntFaks74%3D
    • (2009) Development , vol.136 , pp. 1571-1581
    • Jin, S.1    Pan, L.2    Liu, Z.3    Wang, Q.4    Xu, Z.5    Zhang, Y.Q.6
  • 47
    • 37249041898 scopus 로고    scopus 로고
    • Synthetic lethal interactions identify phenotypic "interologs" of the spindle assembly checkpoint components
    • DOI 10.1534/genetics.107.080408
    • M Tarailo S Tarailo AM Rose 2007 Synthetic lethal interactions identify phenotypic "interologs" of the spindle assembly checkpoint components Genetics 177 2525 2530 10.1534/genetics.107.080408 18073444 1:CAS:528: DC%2BD1cXhtlCjt70%3D (Pubitemid 350277024)
    • (2007) Genetics , vol.177 , Issue.4 , pp. 2525-2530
    • Tarailo, M.1    Tarailo, S.2    Rose, A.M.3
  • 48
    • 4143061786 scopus 로고    scopus 로고
    • Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A
    • DOI 10.1016/j.jmb.2004.06.057, PII S0022283604007612
    • S Raasi I Orlov KG Fleming CM Pickart 2004 Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A J Mol Biol 341 1367 1379 10.1016/j.jmb.2004.06.057 15321727 1:CAS:528:DC%2BD2cXmsVCrtbo%3D (Pubitemid 39092321)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1367-1379
    • Raasi, S.1    Orlov, I.2    Fleming, K.G.3    Pickart, C.M.4
  • 49
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • 8887631
    • S van Nocker S Sadis DM Rubin M Glickman H Fu O Coux I Wefes D Finley RD Vierstra 1996 The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover Mol Cell Biol 16 6020 6028 8887631
    • (1996) Mol Cell Biol , vol.16 , pp. 6020-6028
    • Van Nocker, S.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 50
    • 0031890210 scopus 로고    scopus 로고
    • Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1
    • DOI 10.1074/jbc.273.4.1970
    • H Fu S Sadis DM Rubin M Glickman S van Nocker D Finley RD Vierstra 1998 Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1 J Biol Chem 273 1970 1981 10.1074/jbc.273.4.1970 9442033 1:CAS:528:DyaK1cXnsVCktQ%3D%3D (Pubitemid 28069242)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.4 , pp. 1970-1981
    • Fu, H.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Van Nocker, S.5    Finley, D.6    Vierstra, R.D.7
  • 51
    • 17044368771 scopus 로고    scopus 로고
    • The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation
    • 10.1016/j.molcel.2005.03.015 15837425 1:CAS:528:DC%2BD2MXjvFSrsLw%3D
    • S Heessen MG Masucci NP Dantuma 2005 The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation Mol Cell 18 225 235 10.1016/j.molcel.2005.03.015 15837425 1:CAS:528: DC%2BD2MXjvFSrsLw%3D
    • (2005) Mol Cell , vol.18 , pp. 225-235
    • Heessen, S.1    Masucci, M.G.2    Dantuma, N.P.3
  • 52
    • 20444384069 scopus 로고    scopus 로고
    • Analysis of polybiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets
    • DOI 10.1074/mcp.M400220-MCP200
    • T Mayor JR Lipford J Graumann GT Smith RJ Deshaies 2005 Analysis of polyubiquitin conjugates reveals that the rpn10 substrate receptor contributes to the turnover of multiple proteasome targets Mol Cell Proteomics 4 741 751 10.1074/mcp.M400220-MCP200 15699485 1:CAS:528:DC%2BD2MXlsV2nsr0%3D (Pubitemid 40873003)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.6 , pp. 741-751
    • Mayor, T.1    Lipford, J.R.2    Graumann, J.3    Smith, G.T.4    Deshaies, R.J.5
  • 53
    • 1842472483 scopus 로고    scopus 로고
    • Caspase activation inhibits proteasome function during apoptosis
    • DOI 10.1016/S1097-2765(04)00156-X, PII S109727650400156X
    • XM Sun M Butterworth M MacFarlane W Dubiel A Ciechanover GM Cohen 2004 Caspase activation inhibits proteasome function during apoptosis Mol Cell 14 81 93 10.1016/S1097-2765(04)00156-X 15068805 1:CAS:528:DC%2BD2cXjvVaqtr8%3D (Pubitemid 38469911)
    • (2004) Molecular Cell , vol.14 , Issue.1 , pp. 81-93
    • Sun, X.-M.1    Butterworth, M.2    MacFarlane, M.3    Dubiel, W.4    Ciechanover, A.5    Cohen, G.M.6
  • 55
    • 0034614416 scopus 로고    scopus 로고
    • Activity and regulation of the centrosome-associated proteasome
    • DOI 10.1074/jbc.275.1.409
    • RP Fabunmi WC Wigley PJ Thomas GN DeMartino 2000 Activity and regulation of the centrosome-associated proteasome J Biol Chem 275 409 413 10.1074/jbc.275.1.409 10617632 1:CAS:528:DC%2BD3cXjvVKisg%3D%3D (Pubitemid 30038999)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.1 , pp. 409-413
    • Fabunmi, R.P.1    Wigley, W.C.2    Thomas, P.J.3    DeMartino, G.N.4
  • 56
    • 0034597590 scopus 로고    scopus 로고
    • Centrosomes have a role in regulating the destruction of cyclin B in early Drosophila embryos
    • 10.1016/S0960-9822(00)00776-4 11084336 1:CAS:528:DC%2BD3cXotVOht74%3D
    • JG Wakefield JY Huang JW Raff 2000 Centrosomes have a role in regulating the destruction of cyclin B in early Drosophila embryos Curr Biol 10 1367 1370 10.1016/S0960-9822(00)00776-4 11084336 1:CAS:528:DC%2BD3cXotVOht74%3D
    • (2000) Curr Biol , vol.10 , pp. 1367-1370
    • Wakefield, J.G.1    Huang, J.Y.2    Raff, J.W.3
  • 57
    • 16344379858 scopus 로고    scopus 로고
    • Dynamic recruitment of Nek2 kinase to the centrosome involves microtubules, PCM-1, and localized proteasomal degradation
    • DOI 10.1091/mbc.E04-08-0688
    • RS Hames RE Crookes KR Straatman A Merdes MJ Hayes AJ Faragher AM Fry 2005 Dynamic recruitment of Nek2 kinase to the centrosome involves microtubules, PCM-1, and localized proteasomal degradation Mol Biol Cell 16 1711 1724 10.1091/mbc.E04-08-0688 15659651 1:CAS:528:DC%2BD2MXjt1Kqt7s%3D (Pubitemid 40471942)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.4 , pp. 1711-1724
    • Hames, R.S.1    Crookes, R.E.2    Straatman, K.R.3    Merdes, A.4    Hayes, M.J.5    Faragher, A.J.6    Fry, A.M.7
  • 58
    • 20444451210 scopus 로고    scopus 로고
    • Parkin stabilizes microtubules through strong binding mediated by three independent domains
    • DOI 10.1074/jbc.M500843200
    • F Yang Q Jiang J Zhao Y Ren MD Sutton J Feng 2005 Parkin stabilizes microtubules through strong binding mediated by three independent domains J Biol Chem 280 17154 17162 10.1074/jbc.M500843200 15737990 1:CAS:528: DC%2BD2MXjsFOgtLk%3D (Pubitemid 41389181)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17154-17162
    • Yang, F.1    Jiang, Q.2    Zhao, J.3    Ren, Y.4    Sutton, M.D.5    Feng, J.6
  • 59
    • 0142074728 scopus 로고    scopus 로고
    • Parkin is recruited to the centrosome in response to inhibition of proteasomes
    • DOI 10.1242/jcs.00700
    • J Zhao Y Ren Q Jiang J Feng 2003 Parkin is recruited to the centrosome in response to inhibition of proteasomes J Cell Sci 116 4011 4019 10.1242/jcs.00700 12928331 1:CAS:528:DC%2BD3sXosFCrsLo%3D (Pubitemid 37279315)
    • (2003) Journal of Cell Science , vol.116 , Issue.19 , pp. 4011-4019
    • Zhao, J.1    Ren, Y.2    Jiang, Q.3    Feng, J.4
  • 60
    • 33645778345 scopus 로고    scopus 로고
    • Genetic analysis of the cytoplasmic dynein subunit families
    • 10.1371/journal.pgen.0020001 16440056 1:CAS:528:DC%2BD28XhtVOnsLw%3D
    • KK Pfister PR Shah H Hummerich A Russ J Cotton AA Annuar SM King EM Fisher 2006 Genetic analysis of the cytoplasmic dynein subunit families PLoS Genet 2 e1 10.1371/journal.pgen.0020001 16440056 1:CAS:528:DC%2BD28XhtVOnsLw%3D
    • (2006) PLoS Genet , vol.2 , pp. 1
    • Pfister, K.K.1    Shah, P.R.2    Hummerich, H.3    Russ, A.4    Cotton, J.5    Annuar, A.A.6    King, S.M.7    Fisher, E.M.8


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