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Volumn 7, Issue 11, 2012, Pages

HUWE1 and TRIP12 Collaborate in Degradation of Ubiquitin-Fusion Proteins and Misframed Ubiquitin

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; PROTEASOME; PROTEIN P97; SMALL INTERFERING RNA; UBIQUITIN FUSION PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84870260178     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0050548     Document Type: Article
Times cited : (31)

References (30)
  • 1
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman MH, Ciechanover A, (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82: 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 2
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, et al. (1999) A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96: 635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5
  • 3
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D, Kumar S, (2009) Physiological functions of the HECT family of ubiquitin ligases. Nat Rev Mol Cell Biol 10: 398-409.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 4
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbe S, (2009) Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 10: 550-563.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 5
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D, (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78: 477-513.
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 6
    • 1042278905 scopus 로고    scopus 로고
    • Proteasome and peptidase function in MHC-class-I-mediated antigen presentation
    • Kloetzel PM, Ossendorp F, (2004) Proteasome and peptidase function in MHC-class-I-mediated antigen presentation. Curr Opin Immunol 16: 76-81.
    • (2004) Curr Opin Immunol , vol.16 , pp. 76-81
    • Kloetzel, P.M.1    Ossendorp, F.2
  • 7
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson ES, Ma PC, Ota IM, Varshavsky A, (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J Biol Chem 270: 17442-17456.
    • (1995) J Biol Chem , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 8
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma NP, Lindsten K, Glas R, Jellne M, Masucci MG, (2000) Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells. Nat Biotechnol 18: 538-543.
    • (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
  • 9
    • 0034646298 scopus 로고    scopus 로고
    • Physical association of ubiquitin ligases and the 26S proteasome
    • Xie Y, Varshavsky A, (2000) Physical association of ubiquitin ligases and the 26S proteasome. Proc Natl Acad Sci U S A 97: 2497-2502.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 2497-2502
    • Xie, Y.1    Varshavsky, A.2
  • 10
    • 0029814693 scopus 로고    scopus 로고
    • Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae
    • Ghislain M, Dohmen RJ, Levy F, Varshavsky A, (1996) Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J 15: 4884-4899.
    • (1996) EMBO J , vol.15 , pp. 4884-4899
    • Ghislain, M.1    Dohmen, R.J.2    Levy, F.3    Varshavsky, A.4
  • 11
    • 59449107923 scopus 로고    scopus 로고
    • The HECT domain of TRIP12 ubiquitinates substrates of the ubiquitin fusion degradation pathway
    • Park Y, Yoon SK, Yoon JB, (2009) The HECT domain of TRIP12 ubiquitinates substrates of the ubiquitin fusion degradation pathway. J Biol Chem 284: 1540-1549.
    • (2009) J Biol Chem , vol.284 , pp. 1540-1549
    • Park, Y.1    Yoon, S.K.2    Yoon, J.B.3
  • 12
    • 6844258835 scopus 로고    scopus 로고
    • Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients
    • Van Leeuwen FW, de Kleijn DP, van den Hurk HH, Neubauer A, Sonnemans MA, et al. (1998) Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 279: 242-247.
    • (1998) Science , vol.279 , pp. 242-247
    • van Leeuwen, F.W.1    de Kleijn, D.P.2    van den Hurk, H.H.3    Neubauer, A.4    Sonnemans, M.A.5
  • 13
    • 84880188650 scopus 로고    scopus 로고
    • Frameshift proteins in Alzheimer's disease and in other conformational disorders: time for the ubiquitin-proteasome system
    • Van Leeuwen FW, Hol EM, Fischer DF, (2006) Frameshift proteins in Alzheimer's disease and in other conformational disorders: time for the ubiquitin-proteasome system. J Alzheimers Dis 9: 319-325.
    • (2006) J Alzheimers Dis , vol.9 , pp. 319-325
    • van Leeuwen, F.W.1    Hol, E.M.2    Fischer, D.F.3
  • 14
    • 0037193469 scopus 로고    scopus 로고
    • Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
    • Lindsten K, de Vrij FM, Verhoef LG, Fischer DF, Van Leeuwen FW, et al. (2002) Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J Cell Biol 157: 417-427.
    • (2002) J Cell Biol , vol.157 , pp. 417-427
    • Lindsten, K.1    de Vrij, F.M.2    Verhoef, L.G.3    Fischer, D.F.4    van Leeuwen, F.W.5
  • 15
    • 34249713085 scopus 로고    scopus 로고
    • Dose-dependent inhibition of proteasome activity by a mutant ubiquitin associated with neurodegenerative disease
    • van Tijn P, de Vrij FM, Schuurman KG, Dantuma NP, Fischer DF, et al. (2007) Dose-dependent inhibition of proteasome activity by a mutant ubiquitin associated with neurodegenerative disease. J Cell Sci 120: 1615-1623.
    • (2007) J Cell Sci , vol.120 , pp. 1615-1623
    • van Tijn, P.1    de Vrij, F.M.2    Schuurman, K.G.3    Dantuma, N.P.4    Fischer, D.F.5
  • 16
    • 2342511583 scopus 로고    scopus 로고
    • The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes
    • Hartmann-Petersen R, Wallace M, Hofmann K, Koch G, Johnsen AH, et al. (2004) The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes. Curr Biol 14: 824-828.
    • (2004) Curr Biol , vol.14 , pp. 824-828
    • Hartmann-Petersen, R.1    Wallace, M.2    Hofmann, K.3    Koch, G.4    Johnsen, A.H.5
  • 17
    • 35348953150 scopus 로고    scopus 로고
    • Regulated expression of the ubiquitin protein ligase, E3(Histone)/LASU1/Mule/ARF-BP1/HUWE1, during spermatogenesis
    • Liu Z, Miao D, Xia Q, Hermo L, Wing SS, (2007) Regulated expression of the ubiquitin protein ligase, E3(Histone)/LASU1/Mule/ARF-BP1/HUWE1, during spermatogenesis. Dev Dyn 236: 2889-2898.
    • (2007) Dev Dyn , vol.236 , pp. 2889-2898
    • Liu, Z.1    Miao, D.2    Xia, Q.3    Hermo, L.4    Wing, S.S.5
  • 18
  • 19
    • 67649359951 scopus 로고    scopus 로고
    • Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasome
    • Andersen KM, Madsen L, Prag S, Johnsen AH, Semple CA, et al. (2009) Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasome. J Biol Chem 284: 15246-15254.
    • (2009) J Biol Chem , vol.284 , pp. 15246-15254
    • Andersen, K.M.1    Madsen, L.2    Prag, S.3    Johnsen, A.H.4    Semple, C.A.5
  • 20
    • 35848929692 scopus 로고    scopus 로고
    • A probability-based approach for the analysis of large-scale RNAi screens
    • Konig R, Chiang CY, Tu BP, Yan SF, DeJesus PD, et al. (2007) A probability-based approach for the analysis of large-scale RNAi screens. Nat Methods 4: 847-849.
    • (2007) Nat Methods , vol.4 , pp. 847-849
    • Konig, R.1    Chiang, C.Y.2    Tu, B.P.3    Yan, S.F.4    DeJesus, P.D.5
  • 21
    • 18044364830 scopus 로고    scopus 로고
    • Post-translational regulation in plants employing a diverse set of polypeptide tags
    • Downes B, Vierstra RD, (2005) Post-translational regulation in plants employing a diverse set of polypeptide tags. Biochem Soc Trans 33: 393-399.
    • (2005) Biochem Soc Trans , vol.33 , pp. 393-399
    • Downes, B.1    Vierstra, R.D.2
  • 22
    • 80052728974 scopus 로고    scopus 로고
    • p53 regulation by ubiquitin
    • Brooks CL, Gu W, (2011) p53 regulation by ubiquitin. FEBS Lett 585: 2803-2809.
    • (2011) FEBS Lett , vol.585 , pp. 2803-2809
    • Brooks, C.L.1    Gu, W.2
  • 23
    • 84857411692 scopus 로고    scopus 로고
    • Identification of Mammalian protein quality control factors by high-throughput cellular imaging
    • Pegoraro G, Voss TC, Martin SE, Tuzmen P, Guha R, et al. (2012) Identification of Mammalian protein quality control factors by high-throughput cellular imaging. PLoS One 7: e31684.
    • (2012) PLoS One , vol.7
    • Pegoraro, G.1    Voss, T.C.2    Martin, S.E.3    Tuzmen, P.4    Guha, R.5
  • 24
    • 40749130484 scopus 로고    scopus 로고
    • Submicroscopic duplications of the hydroxysteroid dehydrogenase HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with mental retardation
    • Froyen G, Corbett M, Vandewalle J, Jarvela I, Lawrence O, et al. (2008) Submicroscopic duplications of the hydroxysteroid dehydrogenase HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with mental retardation. Am J Hum Genet 82: 432-443.
    • (2008) Am J Hum Genet , vol.82 , pp. 432-443
    • Froyen, G.1    Corbett, M.2    Vandewalle, J.3    Jarvela, I.4    Lawrence, O.5
  • 25
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • Zhong Q, Gao W, Du F, Wang X, (2005) Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 121: 1085-1095.
    • (2005) Cell , vol.121 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4
  • 26
  • 27
    • 15044354179 scopus 로고    scopus 로고
    • Characterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones
    • Liu Z, Oughtred R, Wing SS, (2005) Characterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones. Mol Cell Biol 25: 2819-2831.
    • (2005) Mol Cell Biol , vol.25 , pp. 2819-2831
    • Liu, Z.1    Oughtred, R.2    Wing, S.S.3
  • 28
    • 73849083434 scopus 로고    scopus 로고
    • Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
    • Schwickart M, Huang X, Lill JR, Liu J, Ferrando R, et al. (2010) Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 463: 103-107.
    • (2010) Nature , vol.463 , pp. 103-107
    • Schwickart, M.1    Huang, X.2    Lill, J.R.3    Liu, J.4    Ferrando, R.5
  • 29
    • 77949323346 scopus 로고    scopus 로고
    • A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities
    • Pandya RK, Partridge JR, Love KR, Schwartz TU, Ploegh HL, (2010) A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities. J Biol Chem 285: 5664-5673.
    • (2010) J Biol Chem , vol.285 , pp. 5664-5673
    • Pandya, R.K.1    Partridge, J.R.2    Love, K.R.3    Schwartz, T.U.4    Ploegh, H.L.5
  • 30
    • 77953467032 scopus 로고    scopus 로고
    • Characterization of the Brain 26S Proteasome and its Interacting Proteins
    • Tai HC, Besche H, Goldberg AL, Schuman EM, (2010) Characterization of the Brain 26S Proteasome and its Interacting Proteins. Front Mol Neurosci 3: 12.
    • (2010) Front Mol Neurosci , vol.3 , pp. 12
    • Tai, H.C.1    Besche, H.2    Goldberg, A.L.3    Schuman, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.