메뉴 건너뛰기




Volumn 10, Issue 5, 2011, Pages

A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE DERIVATIVE; PROTEASOME; RSP5 E3 UBIQUITIN LIGASE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; LYSINE; MUTANT PROTEIN; PROTEOME; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITINATED PROTEIN;

EID: 79955780837     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.009753     Document Type: Article
Times cited : (111)

References (125)
  • 1
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke, L., and Dunn, R. (2003) Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 19, 141-172
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 2
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series
    • Ikeda, F., and Dikic, I. (2008) Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series. EMBO Rep. 9, 536-542
    • (2008) EMBO Rep. , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 3
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • DOI 10.1126/science.1127085
    • Mukhopadhyay, D., and Riezman, H. (2007) Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 315, 201-205 (Pubitemid 46166358)
    • (2007) Science , vol.315 , Issue.5809 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 4
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • Pickart, C. M., and Fushman, D. (2004) Polyubiquitin chains: polymeric protein signals. Curr. Opin. Chem. Biol. 8, 610-616
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 5
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H., and 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
  • 6
    • 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
  • 7
    • 49249120530 scopus 로고    scopus 로고
    • Polyubiquitin chains: Functions, structures, and mechanisms
    • Li, W., and Ye, Y. (2008) Polyubiquitin chains: functions, structures, and mechanisms. Cell Mol. Life Sci. 65, 2397-2406
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 2397-2406
    • Li, W.1    Ye, Y.2
  • 8
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, J., Hochstrasser, M., Finley, D., and Peng, J. (2009) Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137, 133-145
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5    Robert, J.6    Rush, J.7    Hochstrasser, M.8    Finley, D.9    Peng, J.10
  • 9
    • 44949142293 scopus 로고    scopus 로고
    • Systematic approach for validating the ubiquitinated proteome
    • Seyfried, N. T., Xu, P., Duong, D. M., Cheng, D., Hanfelt, J., and Peng, J. (2008) Systematic approach for validating the ubiquitinated proteome. Anal. Chem. 80, 4161-4169
    • (2008) Anal. Chem. , vol.80 , pp. 4161-4169
    • Seyfried, N.T.1    Xu, P.2    Duong, D.M.3    Cheng, D.4    Hanfelt, J.5    Peng, J.6
  • 10
    • 23144452492 scopus 로고    scopus 로고
    • Weighing in on ubiquitin: The expanding role of mass-spectrometry-based proteomics
    • Kirkpatrick, D. S., Denison, C., and Gygi, S. P. (2005) Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics. Nat. Cell Biol. 7, 750-757
    • (2005) Nat. Cell Biol. , vol.7 , pp. 750-757
    • Kirkpatrick, D.S.1    Denison, C.2    Gygi, S.P.3
  • 11
    • 20044373693 scopus 로고    scopus 로고
    • Proteomic identification of ubiquitinated proteins from human cells expressing His-tagged ubiquitin
    • DOI 10.1002/pmic.200401089
    • Kirkpatrick, D. S., Weldon, S. F., Tsaprailis, G., Liebler, D. C., and Gandolfi, A. J. (2005) Proteomic identification of ubiquitinated proteins from human cells expressing His-tagged ubiquitin. Proteomics 5, 2104-2111 (Pubitemid 40770574)
    • (2005) Proteomics , vol.5 , Issue.8 , pp. 2104-2111
    • Kirkpatrick, D.S.1    Weldon, S.F.2    Tsaprailis, G.3    Liebler, D.C.4    Gandolfi, A.J.5
  • 12
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: A general procedure for the quantification of proteins and post-translational modifications
    • DOI 10.1016/j.ymeth.2004.08.018
    • Kirkpatrick, D. S., Gerber, S. A., and Gygi, S. P. (2005) The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods 35, 265-273 (Pubitemid 40255592)
    • (2005) Methods , vol.35 , Issue.3 SPEC.ISS , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 13
    • 13444254137 scopus 로고    scopus 로고
    • Proteomic insights into ubiquitin and ubiquitin-like proteins
    • Denison, C., Kirkpatrick, D. S., and Gygi, S. P. (2005) Proteomic insights into ubiquitin and ubiquitin-like proteins. Curr. Opin. Chem. Biol. 9, 69-75
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 69-75
    • Denison, C.1    Kirkpatrick, D.S.2    Gygi, S.P.3
  • 14
    • 33645703441 scopus 로고    scopus 로고
    • A tandem affinity tag for two-step purification under fully denaturing conditions: Application in ubiquitin profiling and protein complex identification combined with in vivo crosslinking
    • Tagwerker, C., Flick, K., Cui, M., Guerrero, C., Dou, Y., Auer, B., Baldi, P., Huang, L., and Kaiser, P. (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivo crosslinking. Mol. Cell Proteomics 5, 737-748
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 737-748
    • Tagwerker, C.1    Flick, K.2    Cui, M.3    Guerrero, C.4    Dou, Y.5    Auer, B.6    Baldi, P.7    Huang, L.8    Kaiser, P.9
  • 15
    • 36749080327 scopus 로고    scopus 로고
    • Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway
    • DOI 10.1074/mcp.M700264-MCP200
    • Mayor, T., Graumann, J., Bryan, J., MacCoss, M. J., and Deshaies, R. J. (2007) Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway. Mol. Cell Proteomics 6, 1885-1895 (Pubitemid 350201866)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.11 , pp. 1885-1895
    • Mayor, T.1    Graumann, J.2    Bryan, J.3    MacCoss, M.J.4    Deshaies, R.J.5
  • 16
    • 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
    • Mayor, T., Lipford, J. R., Graumann, J., Smith, G. T., and Deshaies, R. J. (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 (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
  • 19
    • 79955760605 scopus 로고    scopus 로고
    • Ubiquitin and Ubiquitination: An overview of the Ubiquitin-proteasome system for protein degradation
    • Nova science publishers Inc
    • Matiuhin, Y., G. M. H. (2006) Ubiquitin and Ubiquitination: an overview of the Ubiquitin-proteasome system for protein degradation. In: The UPS in the nervous system: from Physiology to Pathology Nova science publishers Inc
    • (2006) The UPS in the Nervous System: From Physiology to Pathology
    • Matiuhin, Y.1    H, G.M.2
  • 21
    • 0028146192 scopus 로고
    • Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
    • Finley, D., Sadis, S., Monia, B. P., Boucher, P., Ecker, D. J., Crooke, S. T., and Chau, V. (1994) Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Mol. Cellular Biol. 14, 5501-5509
    • (1994) Mol. Cellular Biol. , vol.14 , pp. 5501-5509
    • Finley, D.1    Sadis, S.2    Monia, B.P.3    Boucher, P.4    Ecker, D.J.5    Crooke, S.T.6    Chau, V.7
  • 22
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • Thrower, J. S., Hoffman, L., Rechsteiner, M., and Pickart, C. M. (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J. 19, 94-102
    • (2000) EMBO J. , vol.19 , pp. 94-102
    • Thrower, J.S.1    Hoffman, L.2    Rechsteiner, M.3    Pickart, C.M.4
  • 23
    • 33644645948 scopus 로고    scopus 로고
    • Ubiquitin binding in endocytosis-how tight should it be and where does it happen?
    • Madshus, I. H. (2006) Ubiquitin binding in endocytosis-how tight should it be and where does it happen? Traffic 7, 258-261
    • (2006) Traffic , vol.7 , pp. 258-261
    • Madshus, I.H.1
  • 24
    • 33646020366 scopus 로고    scopus 로고
    • Monoubiquitylation: A recurrent theme in membrane protein transport
    • Mosesson, Y., and Yarden, Y. (2006) Monoubiquitylation: a recurrent theme in membrane protein transport. Isr. Med. Assoc. J. 8, 233-237
    • (2006) Isr. Med. Assoc. J. , vol.8 , pp. 233-237
    • Mosesson, Y.1    Yarden, Y.2
  • 25
    • 36248991778 scopus 로고    scopus 로고
    • ESCRTing proteins in the endocytic pathway
    • Saksena, S., Sun, J., Chu, T., and Emr, S. D. (2007) ESCRTing proteins in the endocytic pathway. Trends Biochem. Sci. 32, 561-573
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 561-573
    • Saksena, S.1    Sun, J.2    Chu, T.3    Emr, S.D.4
  • 26
    • 77449127817 scopus 로고    scopus 로고
    • No Splicing, no dicing: Non-proteolytic roles of the ubiquitin-proteasome system in transcription
    • Kodadek, T. (2010) No Splicing, no dicing: non-proteolytic roles of the ubiquitin-proteasome system in transcription. J. Biol. Chem. 285, 2221-2226
    • (2010) J. Biol. Chem. , vol.285 , pp. 2221-2226
    • Kodadek, T.1
  • 27
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V., McEwan, D. G., Novak, I., and Dikic, I. (2009) A role for ubiquitin in selective autophagy. Mol. Cell 34, 259-269
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 28
    • 76449117768 scopus 로고    scopus 로고
    • Ubiquitin and SUMO signalling in DNA repair
    • Thomson, T. M., and Guerra-Rebollo, M. (2010) Ubiquitin and SUMO signalling in DNA repair. Biochem. Soc. Trans. 38, 116-131
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 116-131
    • Thomson, T.M.1    Guerra-Rebollo, M.2
  • 29
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen, Z. J., and Sun, L. J. (2009) Nonproteolytic functions of ubiquitin in cell signaling. Mol. Cell 33, 275-286
    • (2009) Mol. Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 30
    • 33751072638 scopus 로고    scopus 로고
    • Lys63-linked polyubiquitin chains: Linking more than just ubiquitin
    • Kawadler, H., and Yang, X. (2006) Lys63-linked polyubiquitin chains: linking more than just ubiquitin. Cancer Biol. Ther. 5, 1273-1274
    • (2006) Cancer Biol. Ther. , vol.5 , pp. 1273-1274
    • Kawadler, H.1    Yang, X.2
  • 31
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • DOI 10.1038/sj.emboj.7600808, PII 7600808
    • Haglund, K., and Dikic, I. (2005) Ubiquitylation and cell signaling. EMBO J. 24, 3353-3359 (Pubitemid 41486773)
    • (2005) EMBO Journal , vol.24 , Issue.19 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 32
    • 33646147146 scopus 로고    scopus 로고
    • Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules
    • Duncan, L. M., Piper, S., Dodd, R. B., Saville, M. K., Sanderson, C. M., Luzio, J. P., and Lehner, P. J. (2006) Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules. EMBO J. 25, 1635-1645
    • (2006) EMBO J. , vol.25 , pp. 1635-1645
    • Duncan, L.M.1    Piper, S.2    Dodd, R.B.3    Saville, M.K.4    Sanderson, C.M.5    Luzio, J.P.6    Lehner, P.J.7
  • 33
    • 67749127761 scopus 로고    scopus 로고
    • Glucose-induced ubiquitylation and endocytosis of the yeast Jen1 transporter: Role of lysine 63-linked ubiquitin chains
    • Paiva, S., Vieira, N., Nondier, I., Haguenauer-Tsapis, R., Casal, M., and Urban-Grimal, D. (2009) Glucose-induced ubiquitylation and endocytosis of the yeast Jen1 transporter: role of lysine 63-linked ubiquitin chains. J. Biol. Chem. 284, 19228-19236
    • (2009) J. Biol. Chem. , vol.284 , pp. 19228-19236
    • Paiva, S.1    Vieira, N.2    Nondier, I.3    Haguenauer-Tsapis, R.4    Casal, M.5    Urban-Grimal, D.6
  • 34
    • 34948905713 scopus 로고    scopus 로고
    • Plasticity of polyubiquitin recognition as lysosomal targeting signals by the endosomal sorting machinery
    • Barriere, H., Nemes, C., Du, K., and Lukacs, G. L. (2007) Plasticity of polyubiquitin recognition as lysosomal targeting signals by the endosomal sorting machinery. Mol. Biol. Cell 18, 3952-3965
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3952-3965
    • Barriere, H.1    Nemes, C.2    Du, K.3    Lukacs, G.L.4
  • 35
    • 33644852909 scopus 로고    scopus 로고
    • Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain
    • DOI 10.1016/j.molcel.2006.02.018, PII S1097276506001201
    • Huang, F., Kirkpatrick, D., Jiang, X., Gygi, S., and Sorkin, A. (2006) Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol. Cell 21, 737-748 (Pubitemid 43376125)
    • (2006) Molecular Cell , vol.21 , Issue.6 , pp. 737-748
    • Huang, F.1    Kirkpatrick, D.2    Jiang, X.3    Gygi, S.4    Sorkin, A.5
  • 37
    • 26944484011 scopus 로고    scopus 로고
    • Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling
    • Geetha, T., Jiang, J., and Wooten, M. W. (2005) Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling. Mol. Cell 20, 301-312
    • (2005) Mol. Cell , vol.20 , pp. 301-312
    • Geetha, T.1    Jiang, J.2    Wooten, M.W.3
  • 38
    • 41149125522 scopus 로고    scopus 로고
    • Agonist-promoted Lys63-linked polyubiquitination of the human kappa-opioid receptor is involved in receptor down-regulation
    • Li, J. G., Haines, D. S., and Liu-Chen, L. Y. (2008) Agonist-promoted Lys63-linked polyubiquitination of the human kappa-opioid receptor is involved in receptor down-regulation. Mol. Pharmacol. 73, 1319-1330
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1319-1330
    • Li, J.G.1    Haines, D.S.2    Liu-Chen, L.Y.3
  • 42
    • 33845970909 scopus 로고    scopus 로고
    • The deubiquitinating enzyme Ubp2 modulates Rsp5-dependent Lys63-linked polyubiquitin conjugates in Saccharomyces cerevisiae
    • Kee, Y., Muñoz, W., Lyon, N., and Huibregtse, J. M. (2006) The deubiquitinating enzyme Ubp2 modulates Rsp5-dependent Lys63-linked polyubiquitin conjugates in Saccharomyces cerevisiae. J. Biol. Chem. 281, 36724-36731
    • (2006) J. Biol. Chem. , vol.281 , pp. 36724-36731
    • Kee, Y.1    Muñoz, W.2    Lyon, N.3    Huibregtse, J.M.4
  • 43
    • 67649227630 scopus 로고    scopus 로고
    • Polyubiquitination by HECT E3s and the determinants of chain type specificity
    • Kim, H. C., and Huibregtse, J. M. (2009) Polyubiquitination by HECT E3s and the determinants of chain type specificity. Mol. Cell. Biol. 29, 3307-3318
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3307-3318
    • Kim, H.C.1    Huibregtse, J.M.2
  • 44
    • 60549107173 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
    • Saeki, Y., Kudo, T., Sone, T., Kikuchi, Y., Yokosawa, H., Toh-e, A., and Tanaka, K. (2009) Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome. EMBO J. 28, 359-371
    • (2009) EMBO J. , vol.28 , pp. 359-371
    • Saeki, Y.1    Kudo, T.2    Sone, T.3    Kikuchi, Y.4    Yokosawa, H.5    Toh-e, A.6    Tanaka, K.7
  • 45
    • 67349113489 scopus 로고    scopus 로고
    • Ubiquitin ligase adaptors: Regulators of ubiquitylation and endocytosis of plasma membrane proteins
    • Léon, S., and Haguenauer-Tsapis, R. (2009) Ubiquitin ligase adaptors: regulators of ubiquitylation and endocytosis of plasma membrane proteins. Exp. Cell Res. 315, 1574-1583
    • (2009) Exp. Cell Res. , vol.315 , pp. 1574-1583
    • Léon, S.1    Haguenauer-Tsapis, R.2
  • 46
    • 55549102963 scopus 로고    scopus 로고
    • Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface
    • Lin, C. H., MacGurn, J. A., Chu, T., Stefan, C. J., and Emr, S. D. (2008) Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135, 714-725
    • (2008) Cell , vol.135 , pp. 714-725
    • Lin, C.H.1    MacGurn, J.A.2    Chu, T.3    Stefan, C.J.4    Emr, S.D.5
  • 47
    • 33745089231 scopus 로고    scopus 로고
    • Regulation of functional diversity within the Nedd4 family by accessory and adaptor proteins
    • DOI 10.1002/bies.20422
    • Shearwin-Whyatt, L., Dalton, H. E., Foot, N., and Kumar, S. (2006) Regulation of functional diversity within the Nedd4 family by accessory and adaptor proteins. Bioessays 28, 617-628 (Pubitemid 43886187)
    • (2006) BioEssays , vol.28 , Issue.6 , pp. 617-628
    • Shearwin-Whyatt, L.1    Dalton, H.E.2    Foot, N.3    Kumar, S.4
  • 48
    • 62649104153 scopus 로고    scopus 로고
    • K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1
    • Cooper, E. M., Cutcliffe, C., Kristiansen, T. Z., Pandey, A., Pickart, C. M., and Cohen, R. E. (2009) K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1. EMBO J. 28, 621-631
    • (2009) EMBO J. , vol.28 , pp. 621-631
    • Cooper, E.M.1    Cutcliffe, C.2    Kristiansen, T.Z.3    Pandey, A.4    Pickart, C.M.5    Cohen, R.E.6
  • 49
    • 62549161305 scopus 로고    scopus 로고
    • Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80
    • Sims, J. J., and Cohen, R. E. (2009) Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80. Mol. Cell 33, 775-783
    • (2009) Mol. Cell , vol.33 , pp. 775-783
    • Sims, J.J.1    Cohen, R.E.2
  • 52
    • 1042278177 scopus 로고    scopus 로고
    • Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase
    • Nishikawa, H., Ooka, S., Sato, K., Arima, K., Okamoto, J., Klevit, R. E., Fukuda, M., and Ohta, T. (2004) Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase. J. Biol. Chem. 279, 3916-3924
    • (2004) J. Biol. Chem. , vol.279 , pp. 3916-3924
    • Nishikawa, H.1    Ooka, S.2    Sato, K.3    Arima, K.4    Okamoto, J.5    Klevit, R.E.6    Fukuda, M.7    Ohta, T.8
  • 53
    • 0042317328 scopus 로고    scopus 로고
    • The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin
    • Wu-Baer, F., Lagrazon, K., Yuan, W., and Baer, R. (2003) The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. J. Biol. Chem. 278, 34743-34746
    • (2003) J. Biol. Chem. , vol.278 , pp. 34743-34746
    • Wu-Baer, F.1    Lagrazon, K.2    Yuan, W.3    Baer, R.4
  • 54
    • 58149280817 scopus 로고    scopus 로고
    • Lysosomal localization of ubiquitinated Jun requires multiple determinants in a lysine-27-linked polyubiquitin conjugate
    • Ikeda, H., and Kerppola, T. K. (2008) Lysosomal localization of ubiquitinated Jun requires multiple determinants in a lysine-27-linked polyubiquitin conjugate. Mol. Biol. Cell 19, 4588-4601
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4588-4601
    • Ikeda, H.1    Kerppola, T.K.2
  • 55
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E. S., Ma, P. C., Ota, I. M., and 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
  • 56
    • 0033578781 scopus 로고    scopus 로고
    • E2/E3-mediated assembly of lysine 29-linked polyubiquitin chains
    • Mastrandrea, L. D., You, J., Niles, E. G., and Pickart, C. M. (1999) E2/E3-mediated assembly of lysine 29-linked polyubiquitin chains. J. Biol. Chem. 274, 27299-27306
    • (1999) J. Biol. Chem. , vol.274 , pp. 27299-27306
    • Mastrandrea, L.D.1    You, J.2    Niles, E.G.3    Pickart, C.M.4
  • 57
    • 50549100537 scopus 로고    scopus 로고
    • AIP4/Itch regulates Notch receptor degradation in the absence of ligand
    • Chastagner, P., Israël, A., and Brou, C. (2008) AIP4/Itch regulates Notch receptor degradation in the absence of ligand. PLoS One 3, e2735
    • (2008) PLoS One , vol.3
    • Chastagner, P.1    Israël, A.2    Brou, C.3
  • 58
    • 0038394715 scopus 로고    scopus 로고
    • Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
    • Haglund, K., Sigismund, S., Polo, S., Szymkiewicz, I., Di Fiore, P. P., and Dikic, I. (2003) Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat. Cell Biol. 5, 461-466
    • (2003) Nat. Cell Biol. , vol.5 , pp. 461-466
    • Haglund, K.1    Sigismund, S.2    Polo, S.3    Szymkiewicz, I.4    Di Fiore, P.P.5    Dikic, I.6
  • 59
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke, L. (2001) Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2, 195-201
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 60
    • 0035823032 scopus 로고    scopus 로고
    • A New Ticket for Entry into Budding Vesicles-Ubiquitin
    • Hicke, L. (2001) A New Ticket for Entry into Budding Vesicles-Ubiquitin. Cell 106, 527-530
    • (2001) Cell , vol.106 , pp. 527-530
    • Hicke, L.1
  • 61
    • 67650422584 scopus 로고    scopus 로고
    • Nonconformity in ubiquitin compliance
    • Ziv, I., Kleifeld, O., and Glickman, M. (2009) Nonconformity in ubiquitin compliance. EMBO J. 28, 1825-1827
    • (2009) EMBO J. , vol.28 , pp. 1825-1827
    • Ziv, I.1    Kleifeld, O.2    Glickman, M.3
  • 62
    • 34547130325 scopus 로고    scopus 로고
    • Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages
    • Kim, H. T., Kim, K. P., Lledias, F., Kisselev, A. F., Scaglione, K. M., Skowyra, D., Gygi, S. P., and Goldberg, A. L. (2007) Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. J. Biol. Chem. 282, 17375-17386
    • (2007) J. Biol. Chem. , vol.282 , pp. 17375-17386
    • Kim, H.T.1    Kim, K.P.2    Lledias, F.3    Kisselev, A.F.4    Scaglione, K.M.5    Skowyra, D.6    Gygi, S.P.7    Goldberg, A.L.8
  • 63
    • 67649823451 scopus 로고    scopus 로고
    • The ubiquitin-interacting motif protein, S5a, is ubiquitinated by all types of ubiquitin ligases by a mechanism different from typical substrate recognition
    • Uchiki, T., Kim, H. T., Zhai, B., Gygi, S. P., Johnston, J. A., O'Bryan, J. P., and Goldberg, A. L. (2009) The ubiquitin-interacting motif protein, S5a, is ubiquitinated by all types of ubiquitin ligases by a mechanism different from typical substrate recognition. J. Biol. Chem. 284, 12622-12632
    • (2009) J. Biol. Chem. , vol.284 , pp. 12622-12632
    • Uchiki, T.1    Kim, H.T.2    Zhai, B.3    Gygi, S.P.4    Johnston, J.A.5    O'Bryan, J.P.6    Goldberg, A.L.7
  • 64
    • 33751515474 scopus 로고    scopus 로고
    • The Polycomb Protein Ring1B Generates Self Atypical Mixed Ubiquitin Chains Required for Its in Vitro Histone H2A Ligase Activity
    • DOI 10.1016/j.molcel.2006.10.022, PII S1097276506007283
    • Ben-Saadon, R., Zaaroor, D., Ziv, T., and Ciechanover, A. (2006) The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity. Mol. Cell 24, 701-711 (Pubitemid 44839211)
    • (2006) Molecular Cell , vol.24 , Issue.5 , pp. 701-711
    • Ben-Saadon, R.1    Zaaroor, D.2    Ziv, T.3    Ciechanover, A.4
  • 65
    • 73549090361 scopus 로고    scopus 로고
    • Efficient internalization of MHC I requires lysine-11 and lysine-63 mixed linkage polyubiquitin chains
    • Boname, J. M., Thomas, M., Stagg, H. R., Xu, P., Peng, J., and Lehner, P. J. (2010) Efficient internalization of MHC I requires lysine-11 and lysine-63 mixed linkage polyubiquitin chains. Traffic 11, 210-220
    • (2010) Traffic , vol.11 , pp. 210-220
    • Boname, J.M.1    Thomas, M.2    Stagg, H.R.3    Xu, P.4    Peng, J.5    Lehner, P.J.6
  • 67
    • 28744459541 scopus 로고    scopus 로고
    • Chemical and genetic strategies for manipulating polyubiquitin chain structure
    • Volk, S., Wang, M., and Pickart, C. M. (2005) Chemical and genetic strategies for manipulating polyubiquitin chain structure. Methods Enzymol. 399, 3-20
    • (2005) Methods Enzymol. , vol.399 , pp. 3-20
    • Volk, S.1    Wang, M.2    Pickart, C.M.3
  • 68
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • Arnason, T., and Ellison, M. J. (1994) Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell. Biol. 14, 7876-7883
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7876-7883
    • Arnason, T.1    Ellison, M.J.2
  • 69
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence, J., Sadis, S., Haas, A. L., and Finley, D. (1995) A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 15, 1265-1273
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 70
    • 47649108312 scopus 로고    scopus 로고
    • Substrate- and ubiquitin-dependent trafficking of the yeast siderophore transporter Sit1
    • DOI 10.1111/j.1600-0854.2008.00766.x
    • Erpapazoglou, Z., Froissard, M., Nondier, I., Lesuisse, E., Haguenauer-Tsapis, R., and Belgareh-Touzé, N. (2008) Substrate- and ubiquitin-dependent trafficking of the yeast siderophore transporter Sit1. Traffic 9, 1372-1391 (Pubitemid 352016293)
    • (2008) Traffic , vol.9 , Issue.8 , pp. 1372-1391
    • Erpapazoglou, Z.1    Froissard, M.2    Nondier, I.3    Lesuisse, E.4    Haguenauer-Tsapis, R.5    Belgareh-Touze, N.6
  • 71
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan, J. M., and Haguenauer-Tsapis, R. (1997) Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 16, 5847-5854
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 72
    • 65649128660 scopus 로고    scopus 로고
    • K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway
    • Lauwers, E., Jacob, C., and André, B. (2009) K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. J. Cell Biol. 185, 493-502
    • (2009) J. Cell Biol. , vol.185 , pp. 493-502
    • Lauwers, E.1    Jacob, C.2    André, B.3
  • 74
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 77
    • 78649974984 scopus 로고    scopus 로고
    • Dynamics of Cullin-RING Ubiquitin Ligase Network Revealed by Systematic Quantitative Proteomics
    • Bennett, E. J., Rush, J., Gygi, S. P., and Harper, J. W. (2010) Dynamics of Cullin-RING Ubiquitin Ligase Network Revealed by Systematic Quantitative Proteomics. Cell 143, 951-965
    • (2010) Cell , vol.143 , pp. 951-965
    • Bennett, E.J.1    Rush, J.2    Gygi, S.P.3    Harper, J.W.4
  • 78
    • 77953108542 scopus 로고    scopus 로고
    • The diversity of ubiquitin recognition: Hot spots and varied specificity
    • Winget, J. M., and Mayor, T. (2010) The diversity of ubiquitin recognition: hot spots and varied specificity. Mol Cell 38, 627-635
    • (2010) Mol Cell , vol.38 , pp. 627-635
    • Winget, J.M.1    Mayor, T.2
  • 80
    • 77950541324 scopus 로고    scopus 로고
    • Orm1 and Orm2 are conserved endoplasmic reticulum membrane proteins regulating lipid homeostasis and protein quality control
    • Han, S., Lone, M. A., Schneiter, R., and Chang, A. (2010) Orm1 and Orm2 are conserved endoplasmic reticulum membrane proteins regulating lipid homeostasis and protein quality control. Proc. Natl. Acad. Sci. U.S.A. 107, 5851-5856
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5851-5856
    • Han, S.1    Lone, M.A.2    Schneiter, R.3    Chang, A.4
  • 81
    • 0141541745 scopus 로고    scopus 로고
    • The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast
    • Caviston, J. P., Longtine, M., Pringle, J. R., and Bi, E. (2003) The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast. Mol. Biol. Cell 14, 4051-4066
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4051-4066
    • Caviston, J.P.1    Longtine, M.2    Pringle, J.R.3    Bi, E.4
  • 83
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann, D. J., Babst, M., and Emr, S. D. (2001) Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 106, 145-155
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 85
    • 84887212507 scopus 로고    scopus 로고
    • A newly identified essential complex, Dre2-Tah18, controls mitochondria integrity and cell death after oxidative stress in yeast
    • Vernis, L., Facca, C., Delagoutte, E., Soler, N., Chanet, R., Guiard, B., Faye, G., and Baldacci, G. (2009) A newly identified essential complex, Dre2-Tah18, controls mitochondria integrity and cell death after oxidative stress in yeast. PLoS One 4, e4376
    • (2009) PLoS One , vol.4
    • Vernis, L.1    Facca, C.2    Delagoutte, E.3    Soler, N.4    Chanet, R.5    Guiard, B.6    Faye, G.7    Baldacci, G.8
  • 86
    • 0034943323 scopus 로고    scopus 로고
    • The class C Vps complex functions at multiple stages of the vacuolar transport pathway
    • Peterson, M. R., and Emr, S. D. (2001) The class C Vps complex functions at multiple stages of the vacuolar transport pathway. Traffic 2, 476-486
    • (2001) Traffic , vol.2 , pp. 476-486
    • Peterson, M.R.1    Emr, S.D.2
  • 87
    • 77956285483 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of She2p by RNA pol II elongation factor Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud
    • Shen, Z., St-Denis, A., and Chartrand, P. (2010) Cotranscriptional recruitment of She2p by RNA pol II elongation factor Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud. Genes Dev. 24, 1914-1926
    • (2010) Genes Dev. , vol.24 , pp. 1914-1926
    • Shen, Z.1    St-Denis, A.2    Chartrand, P.3
  • 88
    • 11144266855 scopus 로고    scopus 로고
    • The PCNA-RFC families of DNA clamps and clamp loaders
    • Majka, J., and Burgers, P. M. (2004) The PCNA-RFC families of DNA clamps and clamp loaders. Prog Nucleic Acids Res. Mol Biol 78, 227-260
    • (2004) Prog Nucleic Acids Res. Mol Biol , vol.78 , pp. 227-260
    • Majka, J.1    Burgers, P.M.2
  • 89
    • 0345616428 scopus 로고    scopus 로고
    • A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
    • DOI 10.1093/emboj/cdg140
    • Shih, S. C., Prag, G., Francis, S. A., Sutanto, M. A., Hurley, J. H., and Hicke, L. (2003) A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain. EMBO J. 22, 1273-1281 (Pubitemid 36362691)
    • (2003) EMBO Journal , vol.22 , Issue.6 , pp. 1273-1281
    • Shih, S.C.1    Prag, G.2    Francis, S.A.3    Sutanto, M.A.4    Hurley, J.H.5    Hicke, L.6
  • 90
    • 71849101657 scopus 로고    scopus 로고
    • The function of yeast epsin and Ede1 ubiquitin-binding domains during receptor internalization
    • Dores, M. R., Schnell, J. D., Maldonado-Baez, L., Wendland, B., and Hicke, L. (2010) The function of yeast epsin and Ede1 ubiquitin-binding domains during receptor internalization. Traffic 11, 151-160
    • (2010) Traffic , vol.11 , pp. 151-160
    • Dores, M.R.1    Schnell, J.D.2    Maldonado-Baez, L.3    Wendland, B.4    Hicke, L.5
  • 91
    • 1942437556 scopus 로고    scopus 로고
    • The Rsp5 Ubiquitin Ligase Binds to and Ubiquitinates Members of the Yeast CIN85-Endophilin Complex, Sla1-Rvs167
    • DOI 10.1074/jbc.M313479200
    • Stamenova, S. D., Dunn, R., Adler, A. S., and Hicke, L. (2004) The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167. J. Biol. Chem. 279, 16017-16025 (Pubitemid 38509291)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 16017-16025
    • Stamenova, S.D.1    Dunn, R.2    Adler, A.S.3    Hicke, L.4
  • 92
    • 57049101734 scopus 로고    scopus 로고
    • Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1
    • Nikko, E., Sullivan, J. A., and Pelham, H. R. (2008) Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1. EMBO Rep 9, 1216-1221
    • (2008) EMBO Rep , vol.9 , pp. 1216-1221
    • Nikko, E.1    Sullivan, J.A.2    Pelham, H.R.3
  • 93
    • 70649112359 scopus 로고    scopus 로고
    • Arrestin-mediated endocytosis of yeast plasma membrane transporters
    • Nikko, E., and Pelham, H. R. (2009) Arrestin-mediated endocytosis of yeast plasma membrane transporters. Traffic 10, 1856-1867
    • (2009) Traffic , vol.10 , pp. 1856-1867
    • Nikko, E.1    Pelham, H.R.2
  • 94
    • 0032827035 scopus 로고    scopus 로고
    • Rsp5 ubiquitin-protein ligase mediates DNA damage- Induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae
    • Beaudenon, S. L., Huacani, M. R., Wang, G., McDonnell, D. P., and Huibregtse, J. M. (1999) Rsp5 ubiquitin-protein ligase mediates DNA damage- induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae. Mol. Cell. Biol. 19, 6972-6979
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6972-6979
    • Beaudenon, S.L.1    Huacani, M.R.2    Wang, G.3    McDonnell, D.P.4    Huibregtse, J.M.5
  • 95
    • 0032531925 scopus 로고    scopus 로고
    • A novel site for ubiquitination: The N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein
    • DOI 10.1093/emboj/17.20.5964
    • Breitschopf, K., Bengal, E., Ziv, T., Admon, A., and Ciechanover, A. (1998) A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein. EMBO J. 17, 5964-5973 (Pubitemid 28474790)
    • (1998) EMBO Journal , vol.17 , Issue.20 , pp. 5964-5973
    • Breitschopf, K.1    Bengal, E.2    Ziv, T.3    Admon, A.4    Ciechanover, A.5
  • 97
    • 55849153104 scopus 로고    scopus 로고
    • Autophosphorylation- induced degradation of the Pho85 cyclin Pcl5 is essential for response to amino acid limitation
    • Aviram, S., Simon, E., Gildor, T., Glaser, F., and Kornitzer, D. (2008) Autophosphorylation- induced degradation of the Pho85 cyclin Pcl5 is essential for response to amino acid limitation. Mol. Cell. Biol. 28, 6858-6869
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6858-6869
    • Aviram, S.1    Simon, E.2    Gildor, T.3    Glaser, F.4    Kornitzer, D.5
  • 98
    • 70350336434 scopus 로고    scopus 로고
    • Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation
    • Reider, A., Barker, S. L., Mishra, S. K., Im, Y. J., Maldonado- Báez, L., Hurley, J. H., Traub, L. M., and Wendland, B. (2009) Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation. EMBO J. 28, 3103-3116
    • (2009) EMBO J. , vol.28 , pp. 3103-3116
    • Reider, A.1    Barker, S.L.2    Mishra, S.K.3    Im, Y.J.4    Maldonado-Báez, L.5    Hurley, J.H.6    Traub, L.M.7    Wendland, B.8
  • 100
    • 73949119447 scopus 로고    scopus 로고
    • Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast
    • Stimpson, H. E., Toret, C. P., Cheng, A. T., Pauly, B. S., and Drubin, D. G. (2009) Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast. Mol. Biol. Cell 20, 4640-4651
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4640-4651
    • Stimpson, H.E.1    Toret, C.P.2    Cheng, A.T.3    Pauly, B.S.4    Drubin, D.G.5
  • 101
    • 34547843498 scopus 로고    scopus 로고
    • Targeting of Sna3p to the endosomal pathway depends on its interaction with Rsp5p and multivesicular body sorting on its ubiquitylation
    • DOI 10.1111/j.1600-0854.2007.00610.x
    • Stawiecka-Mirota, M., Pokrzywa, W., Morvan, J., Zoladek, T., Haguenauer-Tsapis, R., Urban-Grimal, D., and Morsomme, P. (2007) Targeting of Sna3p to the endosomal pathway depends on its interaction with Rsp5p and multivesicular body sorting on its ubiquitylation. Traffic 8, 1280-1296 (Pubitemid 47244877)
    • (2007) Traffic , vol.8 , Issue.9 , pp. 1280-1296
    • Stawiecka-Mirota, M.1    Pokrzywa, W.2    Morvan, J.3    Zoladek, T.4    Haguenauer-Tsapis, R.5    Urban-Grimal, D.6    Morsomme, P.7
  • 102
  • 103
    • 4344672752 scopus 로고    scopus 로고
    • Antagonistic roles of ESCRT and Vps class C/HOPS complexes in the recycling of yeast membrane proteins
    • Bugnicourt, A., Froissard, M., Sereti, K., Ulrich, H. D., Haguenauer-Tsapis, R., and Galan, J. M. (2004) Antagonistic roles of ESCRT and Vps class C/HOPS complexes in the recycling of yeast membrane proteins. Mol. Biol. Cell 15, 4203-4214
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4203-4214
    • Bugnicourt, A.1    Froissard, M.2    Sereti, K.3    Ulrich, H.D.4    Haguenauer-Tsapis, R.5    Galan, J.M.6
  • 104
    • 0014033501 scopus 로고
    • Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. I. Evidence for a specific arginine-transporting system
    • Grenson, M., Mousset, M., Wiame, J. M., and Bechet, J. (1966) Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. I. Evidence for a specific arginine-transporting system. Biochim. Biophys. Acta 127, 325-338
    • (1966) Biochim. Biophys. Acta , vol.127 , pp. 325-338
    • Grenson, M.1    Mousset, M.2    Wiame, J.M.3    Bechet, J.4
  • 105
    • 47149118006 scopus 로고    scopus 로고
    • Membrane transporters and protein traffic networks differentially affecting metal tolerance: A genomic phenotyping study in yeast
    • Ruotolo, R., Marchini, G., and Ottonello, S. (2008) Membrane transporters and protein traffic networks differentially affecting metal tolerance: a genomic phenotyping study in yeast. Genome Biol. 9, R67
    • (2008) Genome Biol. , vol.9
    • Ruotolo, R.1    Marchini, G.2    Ottonello, S.3
  • 107
    • 0035903635 scopus 로고    scopus 로고
    • Sorting of proteins into multivesicular bodies: Ubiquitin-dependent and -independent targeting
    • Reggiori, F., and Pelham, H. R. (2001) Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting. EMBO J. 20, 5176-5186
    • (2001) EMBO J. , vol.20 , pp. 5176-5186
    • Reggiori, F.1    Pelham, H.R.2
  • 108
    • 1942439642 scopus 로고    scopus 로고
    • Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins
    • Hettema, E. H., Valdez-Taubas, J., and Pelham, H. R. (2004) Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins. EMBO J. 23, 1279-1288
    • (2004) EMBO J. , vol.23 , pp. 1279-1288
    • Hettema, E.H.1    Valdez-Taubas, J.2    Pelham, H.R.3
  • 109
    • 0036902646 scopus 로고    scopus 로고
    • Receptor down regulation and multivesicular-body sorting
    • Katzmann, D. J., Odorizzi, G., and Emr, S. D. (2002) Receptor down regulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 3, 893-905
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 110
    • 79955752057 scopus 로고    scopus 로고
    • A novel strategy to isolate ubiquitin conjugates reveals wide role of ubiquitination during neural development
    • Franco, M., Seyfried, N. T., Brand, A. H., Peng, J., and Mayor, U. (2010) A novel strategy to isolate ubiquitin conjugates reveals wide role of ubiquitination during neural development. Mol. Cell Proteomics
    • (2010) Mol. Cell Proteomics
    • Franco, M.1    Seyfried, N.T.2    Brand, A.H.3    Peng, J.4    Mayor, U.5
  • 112
    • 76549089605 scopus 로고    scopus 로고
    • UBE2S drives elongation of K11-linked ubiquitin chains by the anaphase-promoting complex
    • Wu, T., Merbl, Y., Huo, Y., Gallop, J. L., Tzur, A., and Kirschner, M. W. (2010) UBE2S drives elongation of K11-linked ubiquitin chains by the anaphase-promoting complex. Proc. Natl. Acad. Sci. U.S.A. 107, 1355-1360
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1355-1360
    • Wu, T.1    Merbl, Y.2    Huo, Y.3    Gallop, J.L.4    Tzur, A.5    Kirschner, M.W.6
  • 113
    • 60849126138 scopus 로고    scopus 로고
    • Modification by single ubiquitin moieties rather than polyubiquitination is sufficient for proteasomal processing of the p105 NF-kappaB precursor
    • Kravtsova-Ivantsiv, Y., Cohen, S., and Ciechanover, A. (2009) Modification by single ubiquitin moieties rather than polyubiquitination is sufficient for proteasomal processing of the p105 NF-kappaB precursor. Mol. Cell 33, 496-504
    • (2009) Mol. Cell , vol.33 , pp. 496-504
    • Kravtsova-Ivantsiv, Y.1    Cohen, S.2    Ciechanover, A.3
  • 114
    • 0347087494 scopus 로고    scopus 로고
    • Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome
    • Guterman, A., and Glickman, M. H. (2004) Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. J. Biol. Chem. 279, 1729-1738
    • (2004) J. Biol. Chem. , vol.279 , pp. 1729-1738
    • Guterman, A.1    Glickman, M.H.2
  • 115
    • 0021813071 scopus 로고
    • Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates
    • Hershko, A., and Heller, H. (1985) Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates. Biochem. Biophys. Res. Commun. 128, 1079-1086
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 1079-1086
    • Hershko, A.1    Heller, H.2
  • 116
    • 1542373897 scopus 로고    scopus 로고
    • Distinct monoubiquitin signals in receptor endocytosis
    • Haglund, K., Di Fiore, P. P., and Dikic, I. (2003) Distinct monoubiquitin signals in receptor endocytosis. Trends Biochem. Sci. 28, 598-603
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 598-603
    • Haglund, K.1    Di Fiore, P.P.2    Dikic, I.3
  • 117
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., and Varshavsky, A. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243, 1576-1583 (Pubitemid 19090506)
    • (1989) Science , vol.243 , Issue.4898 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 118
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
    • Spence, J., Gali, R. R., Dittmar, G., Sherman, F., Karin, M., and Finley, D. (2000) Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain. Cell 102, 67-76
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1    Gali, R.R.2    Dittmar, G.3    Sherman, F.4    Karin, M.5    Finley, D.6
  • 119
    • 34547920328 scopus 로고    scopus 로고
    • Split-ubiquitin two-hybrid assay to analyze protein-protein interactions at the endosome: Application to Saccharomyces cerevisiae Bro1 interacting with ESCRT complexes, the Doa4 ubiquitin hydrolase, and the Rsp5 ubiquitin ligase
    • DOI 10.1128/EC.00024-07
    • Nikko, E., and André, B. (2007) Split-ubiquitin two-hybrid assay to analyze protein-protein interactions at the endosome: application to Saccharomyces cerevisiae Bro1 interacting with ESCRT complexes, the Doa4 ubiquitin hydrolase, and the Rsp5 ubiquitin ligase. Eukaryot. Cell 6, 1266-1277 (Pubitemid 47257696)
    • (2007) Eukaryotic Cell , vol.6 , Issue.8 , pp. 1266-1277
    • Nikko, E.1    Andre, B.2
  • 120
    • 77954626403 scopus 로고    scopus 로고
    • Arrestin-2 interacts with the endosomal sorting complex required for transport machinery to modulate endosomal sorting of CXCR4
    • Malik, R., and Marchese, A. (2010) Arrestin-2 interacts with the endosomal sorting complex required for transport machinery to modulate endosomal sorting of CXCR4. Mol. Biol. Cell 21, 2529-2541
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2529-2541
    • Malik, R.1    Marchese, A.2
  • 121
    • 77951533710 scopus 로고    scopus 로고
    • AMSH interacts with ESCRT-0 to regulate the stability and trafficking of CXCR4
    • Sierra, M. I., Wright, M. H., and Nash, P. D. (2010) AMSH interacts with ESCRT-0 to regulate the stability and trafficking of CXCR4. J. Biol. Chem. 285, 13990-14004
    • (2010) J. Biol. Chem. , vol.285 , pp. 13990-14004
    • Sierra, M.I.1    Wright, M.H.2    Nash, P.D.3
  • 122
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • DOI 10.1083/jcb.200401141
    • McCullough, J., Clague, M. J., and Urbé, S. (2004) AMSH is an endosome-associated ubiquitin isopeptidase. J. Cell Biol. 166, 487-492 (Pubitemid 39097168)
    • (2004) Journal of Cell Biology , vol.166 , Issue.4 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 123
    • 0036786951 scopus 로고    scopus 로고
    • Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae
    • Kamińska, J., Gajewska, B., Hopper, A. K., and Zoladek, T. (2002) Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 22, 6946-6948
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6946-6948
    • Kamińska, J.1    Gajewska, B.2    Hopper, A.K.3    Zoladek, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.