메뉴 건너뛰기




Volumn 292, Issue 25, 2017, Pages 10398-10413

Mechanism of ubiquitin chain synthesis employed by a HECT domain ubiquitin ligase

Author keywords

[No Author keywords available]

Indexed keywords

C (PROGRAMMING LANGUAGE); ENZYMES;

EID: 85021679701     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M117.789479     Document Type: Article
Times cited : (55)

References (72)
  • 2
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation–The unexplored world of polyubiquitin beyond lys48 and lys63 linkages
    • Kulathu, Y., and Komander, D. (2012) Atypical ubiquitylation–the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat. Rev. Mol. Cell Biol. 13, 508 –523
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 3
    • 84861783400 scopus 로고    scopus 로고
    • Ubiquitin-binding proteins: Decoders of ubiquitin-mediated cellular functions
    • Husnjak, K., and Dikic, I. (2012) Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions. Annu. Rev. Biochem. 81, 291–322
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 291-322
    • Husnjak, K.1    Dikic, I.2
  • 4
  • 5
    • 84890176335 scopus 로고    scopus 로고
    • Ring-type e3 ligases: Master manipulators of e2 ubiquitin-conjugating enzymes and ubiquitination
    • Metzger, M. B., Pruneda, J. N., Klevit, R. E., and Weissman, A. M. (2014) RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochim. Biophys. Acta 1843, 47– 60
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 47-60
    • Metzger, M.B.1    Pruneda, J.N.2    Klevit, R.E.3    Weissman, A.M.4
  • 6
    • 84898754901 scopus 로고    scopus 로고
    • New insights into ubiquitin e3 ligase mechanism
    • Berndsen, C. E., and Wolberger, C. (2014) New insights into ubiquitin E3 ligase mechanism. Nat. Struct. Mol. Biol. 21, 301–307
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 301-307
    • Berndsen, C.E.1    Wolberger, C.2
  • 7
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the hect family of ubiquitin ligases
    • Rotin, D., and 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
  • 8
    • 84898614605 scopus 로고    scopus 로고
    • Rbr e3-ligases at work
    • Smit, J. J., and Sixma, T. K. (2014) RBR E3-ligases at work. EMBO Rep. 15, 142–154
    • (2014) EMBO Rep , vol.15 , pp. 142-154
    • Smit, J.J.1    Sixma, T.K.2
  • 9
    • 84896870884 scopus 로고    scopus 로고
    • Rbr e3 ubiquitin ligases: New structures, new insights, new questions
    • Spratt, D. E., Walden, H., and Shaw, G. S. (2014) RBR E3 ubiquitin ligases: new structures, new insights, new questions. Biochem. J. 458, 421– 437
    • (2014) Biochem. J. , vol.458 , pp. 421-437
    • Spratt, D.E.1    Walden, H.2    Shaw, G.S.3
  • 10
    • 45849153870 scopus 로고    scopus 로고
    • The hect family of e3 ubiquitin ligases: Multiple players in cancer development
    • Bernassola, F., Karin, M., Ciechanover, A., and Melino, G. (2008) The HECT family of E3 ubiquitin ligases: multiple players in cancer development. Cancer Cell 14, 10 –21
    • (2008) Cancer Cell , vol.14 , pp. 10-21
    • Bernassola, F.1    Karin, M.2    Ciechanover, A.3    Melino, G.4
  • 11
    • 84890534490 scopus 로고    scopus 로고
    • Regulation of TGF-β family signalling by ubiquitination and deubiquitination
    • Imamura, T., Oshima, Y., and Hikita, A. (2013) Regulation of TGF- family signalling by ubiquitination and deubiquitination. J. Biochem. 154, 481– 489
    • (2013) J. Biochem. , vol.154 , pp. 481-489
    • Imamura, T.1    Oshima, Y.2    Hikita, A.3
  • 12
    • 84920885165 scopus 로고    scopus 로고
    • Nedd4: The founding member of a family of ubiquitin-protein ligases
    • Boase, N. A., and Kumar, S. (2015) NEDD4: the founding member of a family of ubiquitin-protein ligases. Gene 557, 113–122
    • (2015) Gene , vol.557 , pp. 113-122
    • Boase, N.A.1    Kumar, S.2
  • 13
    • 84929961711 scopus 로고    scopus 로고
    • Multifaceted role of the ubiquitin ligase itch in immune regulation
    • Venuprasad, K., Zeng, M., Baughan, S. L., and Massoumi, R. (2015) Multifaceted role of the ubiquitin ligase Itch in immune regulation. Immunol. Cell Biol. 93, 452– 460
    • (2015) Immunol. Cell Biol. , vol.93 , pp. 452-460
    • Venuprasad, K.1    Zeng, M.2    Baughan, S.L.3    Massoumi, R.4
  • 17
    • 84891957449 scopus 로고    scopus 로고
    • The active form of e6-associated protein (e6ap)/ube3a ubiquitin ligase is an oli-gomer
    • Ronchi, V. P., Klein, J. M., Edwards, D. J., and Haas, A. L. (2014) The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oli-gomer. J. Biol. Chem. 289, 1033–1048
    • (2014) J. Biol. Chem , vol.289 , pp. 1033-1048
    • Ronchi, V.P.1    Klein, J.M.2    Edwards, D.J.3    Haas, A.L.4
  • 18
    • 0037249354 scopus 로고    scopus 로고
    • Conformational flexibility underlies ubiquitin ligation mediated by the wwp1 hect domain e3 ligase
    • Verdecia, M. A., Joazeiro, C. A., Wells, N. J., Ferrer, J. L., Bowman, M. E., Hunter, T., and Noel, J. P. (2003) Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase. Mol. Cell 11, 249 –259
    • (2003) Mol. Cell , vol.11 , pp. 249-259
    • Verdecia, M.A.1    Joazeiro, C.A.2    Wells, N.J.3    Ferrer, J.L.4    Bowman, M.E.5    Hunter, T.6    Noel, J.P.7
  • 19
    • 29244447753 scopus 로고    scopus 로고
    • Different hect domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis
    • Wang, M., and Pickart, C. M. (2005) Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis. EMBO J. 24, 4324 – 4333
    • (2005) EMBO J. , vol.24 , pp. 4324-4333
    • Wang, M.1    Pickart, C.M.2
  • 20
    • 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
  • 21
    • 79953325889 scopus 로고    scopus 로고
    • Structure of the hect: Ubiquitin complex and its role in ubiquitin chain elongation
    • Maspero, E., Mari, S., Valentini, E., Musacchio, A., Fish, A., Pasqualato, S., and Polo, S. (2011) Structure of the HECT: ubiquitin complex and its role in ubiquitin chain elongation. EMBO Rep. 12, 342–349
    • (2011) EMBO Rep , vol.12 , pp. 342-349
    • Maspero, E.1    Mari, S.2    Valentini, E.3    Musacchio, A.4    Fish, A.5    Pasqualato, S.6    Polo, S.7
  • 22
    • 84876237590 scopus 로고    scopus 로고
    • E6AP/UBE3A ubiquitin ligase harbors two E2ubiquitin binding sites
    • Ronchi, V. P., Klein, J. M., and Haas, A. L. (2013) E6AP/UBE3A ubiquitin ligase harbors two E2ubiquitin binding sites. J. Biol. Chem. 288, 10349 –10360
    • (2013) J. Biol. Chem. , vol.288 , pp. 10349-10360
    • Ronchi, V.P.1    Klein, J.M.2    Haas, A.L.3
  • 23
    • 30344482590 scopus 로고    scopus 로고
    • Lingering mysteries of ubiquitin-chain assembly
    • Hochstrasser, M. (2006) Lingering mysteries of ubiquitin-chain assembly. Cell 124, 27–34
    • (2006) Cell , vol.124 , pp. 27-34
    • Hochstrasser, M.1
  • 24
    • 66449125689 scopus 로고    scopus 로고
    • Regulation of the rsp5 ubiquitin ligase by an intrinsic ubiquitin-binding site
    • French, M. E., Kretzmann, B. R., and Hicke, L. (2009) Regulation of the RSP5 ubiquitin ligase by an intrinsic ubiquitin-binding site. J. Biol. Chem. 284, 12071–12079
    • (2009) J. Biol. Chem. , vol.284 , pp. 12071-12079
    • French, M.E.1    Kretzmann, B.R.2    Hicke, L.3
  • 25
    • 77949888615 scopus 로고    scopus 로고
    • The ubiquitin binding region of the smurf hect domain facilitates polyubiquitylation and binding of ubiquitylated substrates
    • Ogunjimi, A. A., Wiesner, S., Briant, D. J., Varelas, X., Sicheri, F., Forman-Kay, J., and Wrana, J. L. (2010) The ubiquitin binding region of the Smurf HECT domain facilitates polyubiquitylation and binding of ubiquitylated substrates. J. Biol. Chem. 285, 6308 – 6315
    • (2010) J. Biol. Chem. , vol.285 , pp. 6308-6315
    • Ogunjimi, A.A.1    Wiesner, S.2    Briant, D.J.3    Varelas, X.4    Sicheri, F.5    Forman-Kay, J.6    Wrana, J.L.7
  • 26
    • 79953310074 scopus 로고    scopus 로고
    • Structure and function of a hect domain ubiquitin-binding site
    • Kim, H. C., Steffen, A. M., Oldham, M. L., Chen, J., and Huibregtse, J. M. (2011) Structure and function of a HECT domain ubiquitin-binding site. EMBO Rep. 12, 334 –341
    • (2011) EMBO Rep , vol.12 , pp. 334-341
    • Kim, H.C.1    Steffen, A.M.2    Oldham, M.L.3    Chen, J.4    Huibregtse, J.M.5
  • 28
    • 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
  • 29
    • 54249105821 scopus 로고    scopus 로고
    • Hpv e6, e6ap and cervical cancer
    • Beaudenon, S., and Huibregtse, J. M. (2008) HPV E6, E6AP and cervical cancer. BMC Biochem. 9, Suppl. 1, S4
    • (2008) BMC Biochem , vol.9 , pp. S4
    • Beaudenon, S.1    Huibregtse, J.M.2
  • 32
    • 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
  • 33
    • 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
    • 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
    • (2007) Traffic , vol.8 , 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
  • 35
    • 33750530169 scopus 로고    scopus 로고
    • Itch/aip4 mediates deltex degradation through the formation of lys-29-linked polyubiquitin chains
    • Chastagner, P., Israël, A., and Brou, C. (2006) Itch/AIP4 mediates Deltex degradation through the formation of Lys-29-linked polyubiquitin chains. EMBO Rep. 7, 1147–1153
    • (2006) EMBO Rep , vol.7 , pp. 1147-1153
    • Chastagner, P.1    Israël, A.2    Brou, C.3
  • 36
    • 80052620165 scopus 로고    scopus 로고
    • Smad6-specific recruitment of smurf e3 ligases mediates tgf-1-induced degradation of myd88 in tlr4 signalling
    • Lee, Y. S., Park, J. S., Kim, J. H., Jung, S. M., Lee, J. Y., Kim, S. J., and Park, S. H. (2011) Smad6-specific recruitment of Smurf E3 ligases mediates TGF-1-induced degradation of MyD88 in TLR4 signalling. Nat. Commun. 2, 460
    • (2011) Nat. Commun. , vol.2 , pp. 460
    • Lee, Y.S.1    Park, J.S.2    Kim, J.H.3    Jung, S.M.4    Lee, J.Y.5    Kim, S.J.6    Park, S.H.7
  • 37
    • 84875549688 scopus 로고    scopus 로고
    • E3 ligase wwp2 negatively regulates tlr3-mediated innate immune response by targeting trif for ubiquitination and degradation
    • Yang, Y., Liao, B., Wang, S., Yan, B., Jin, Y., Shu, H. B., and Wang, Y. Y. (2013) E3 ligase WWP2 negatively regulates TLR3-mediated innate immune response by targeting TRIF for ubiquitination and degradation. Proc. Natl. Acad. Sci. U.S.A. 110, 5115–5120
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 5115-5120
    • Yang, Y.1    Liao, B.2    Wang, S.3    Yan, B.4    Jin, Y.5    Shu, H.B.6    Wang, Y.Y.7
  • 39
    • 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
  • 43
    • 84900337781 scopus 로고    scopus 로고
    • Enhanced protein degradation by branched ubiquitin chains
    • Meyer, H. J., and Rape, M. (2014) Enhanced protein degradation by branched ubiquitin chains. Cell 157, 910 –921
    • (2014) Cell , vol.157 , pp. 910-921
    • Meyer, H.J.1    Rape, M.2
  • 44
    • 33646122226 scopus 로고    scopus 로고
    • Molecular determinants of polyubiquitin linkage selection by an hect ubiquitin ligase
    • Wang, M., Cheng, D., Peng, J., and Pickart, C. M. (2006) Molecular determinants of polyubiquitin linkage selection by an HECT ubiquitin ligase. EMBO J. 25, 1710 –1719
    • (2006) EMBO J , vol.25 , pp. 1710-1719
    • Wang, M.1    Cheng, D.2    Peng, J.3    Pickart, C.M.4
  • 45
    • 84877313192 scopus 로고    scopus 로고
    • Assembly, analysis and architecture of atypical ubiquitin chains
    • Hospenthal, M. K., Freund, S. M., and Komander, D. (2013) Assembly, analysis and architecture of atypical ubiquitin chains. Nat. Struct. Mol. Biol. 20, 555–565
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 555-565
    • Hospenthal, M.K.1    Freund, S.M.2    Komander, D.3
  • 46
    • 84905714913 scopus 로고    scopus 로고
    • Middle-down mass spectrometry enables characterization of branched ubiquitin chains
    • Valkevich, E. M., Sanchez, N. A., Ge, Y., and Strieter, E. R. (2014) Middle-down mass spectrometry enables characterization of branched ubiquitin chains. Biochemistry 53, 4979 – 4989
    • (2014) Biochemistry , vol.53 , pp. 4979-4989
    • Valkevich, E.M.1    Sanchez, N.A.2    Ge, Y.3    Strieter, E.R.4
  • 48
    • 77951651753 scopus 로고    scopus 로고
    • The family of ubiquitin-conjugating enzymes (e2s): Deciding between life and death of proteins
    • van Wijk, S. J., and Timmers, H. T. (2010) The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins. FASEB J. 24, 981–993
    • (2010) FASEB J , vol.24 , pp. 981-993
    • Van Wijk, S.J.1    Timmers, H.T.2
  • 50
    • 84943562714 scopus 로고    scopus 로고
    • A small molecule that switches a ubiquitin ligase from a processive to a distributive enzymatic mechanism
    • Kathman, S. G., Span, I., Smith, A. T., Xu, Z., Zhan, J., Rosenzweig, A. C., and Statsyuk, A. V. (2015) A small molecule that switches a ubiquitin ligase from a processive to a distributive enzymatic mechanism. J. Am. Chem. Soc. 137, 12442–12445
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 12442-12445
    • Kathman, S.G.1    Span, I.2    Smith, A.T.3    Xu, Z.4    Zhan, J.5    Rosenzweig, A.C.6    Statsyuk, A.V.7
  • 51
    • 67651004289 scopus 로고    scopus 로고
    • A conserved ubiquitination pathway determines longevity in response to diet restriction
    • Carrano, A. C., Liu, Z., Dillin, A., and Hunter, T. (2009) A conserved ubiquitination pathway determines longevity in response to diet restriction. Nature 460, 396 –399
    • (2009) Nature , vol.460 , pp. 396-399
    • Carrano, A.C.1    Liu, Z.2    Dillin, A.3    Hunter, T.4
  • 52
    • 22744456248 scopus 로고    scopus 로고
    • The rsp5 ubiquitin ligase is coupled to and antagonized by the ubp2 deubiquitinating enzyme
    • Kee, Y., Lyon, N., and Huibregtse, J. M. (2005) The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme. EMBO J. 24, 2414 –2424
    • (2005) EMBO J , vol.24 , pp. 2414-2424
    • Kee, Y.1    Lyon, N.2    Huibregtse, J.M.3
  • 54
    • 80052984488 scopus 로고    scopus 로고
    • Ww domain-containing e3 ubiquitin protein ligase 1 (wwp1) delays cellular senescence by promoting p27(kip1) degradation in human diploid fibroblasts
    • Cao, X., Xue, L., Han, L., Ma, L., Chen, T., and Tong, T. (2011) WW domain-containing E3 ubiquitin protein ligase 1 (WWP1) delays cellular senescence by promoting p27(Kip1) degradation in human diploid fibroblasts. J. Biol. Chem. 286, 33447–33456
    • (2011) J. Biol. Chem. , vol.286 , pp. 33447-33456
    • Cao, X.1    Xue, L.2    Han, L.3    Ma, L.4    Chen, T.5    Tong, T.6
  • 56
    • 77949269474 scopus 로고    scopus 로고
    • Wwp2 mediates oct4 ubiquitination and its own auto-ubiquitination in a dosage-dependent manner
    • Liao, B., and Jin, Y. (2010) Wwp2 mediates Oct4 ubiquitination and its own auto-ubiquitination in a dosage-dependent manner. Cell Res. 20, 332–344
    • (2010) Cell Res , vol.20 , pp. 332-344
    • Liao, B.1    Jin, Y.2
  • 57
    • 71449123070 scopus 로고    scopus 로고
    • Detection of sequential polyubiquitylation on a millisecond timescale
    • Pierce, N. W., Kleiger, G., Shan, S. O., and Deshaies, R. J. (2009) Detection of sequential polyubiquitylation on a millisecond timescale. Nature 462, 615– 619
    • (2009) Nature , vol.462 , pp. 615-619
    • Pierce, N.W.1    Kleiger, G.2    Shan, S.O.3    Deshaies, R.J.4
  • 58
    • 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
  • 59
    • 33847401446 scopus 로고    scopus 로고
    • Regulation of p53 localization and transcription by the HECT domain E3 ligase WWP1
    • Laine, A., and Ronai, Z. (2007) Regulation of p53 localization and transcription by the HECTdomain E3 ligase WWP1. Oncogene 26, 1477–1483
    • (2007) Oncogene , vol.26 , pp. 1477-1483
    • Laine, A.1    Ronai, Z.2
  • 61
    • 77951221830 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitination of the dopamine transporter requires ww3 and ww4 domains of nedd4 –2 and ube2d ubiquitin-conjugating enzymes
    • Vina-Vilaseca, A., and Sorkin, A. (2010) Lysine 63-linked polyubiquitination of the dopamine transporter requires WW3 and WW4 domains of Nedd4 –2 and UBE2D ubiquitin-conjugating enzymes. J. Biol. Chem. 285, 7645–7656
    • (2010) J. Biol. Chem. , vol.285 , pp. 7645-7656
    • Vina-Vilaseca, A.1    Sorkin, A.2
  • 63
    • 84947045877 scopus 로고    scopus 로고
    • The proteasome distinguishes between heterotypic and homo-typic lysine-11-linked polyubiquitin chains
    • Grice, G. L., Lobb, I. T., Weekes, M. P., Gygi, S. P., Antrobus, R., and Nathan, J. A. (2015) The proteasome distinguishes between heterotypic and homo-typic lysine-11-linked polyubiquitin chains. Cell Rep. 12, 545–553
    • (2015) Cell Rep , vol.12 , pp. 545-553
    • Grice, G.L.1    Lobb, I.T.2    Weekes, M.P.3    Gygi, S.P.4    Antrobus, R.5    Nathan, J.A.6
  • 64
    • 33745089231 scopus 로고    scopus 로고
    • Regulation of functional diversity within the nedd4 family by accessory and adaptor proteins
    • 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
    • (2006) Bioessays , vol.28 , pp. 617-628
    • Shearwin-Whyatt, L.1    Dalton, H.E.2    Foot, N.3    Kumar, S.4
  • 65
    • 34347379169 scopus 로고    scopus 로고
    • Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase rsp5 to membrane proteins in vivo and in vitro
    • Sullivan, J. A., Lewis, M. J., Nikko, E., and Pelham, H. R. (2007) Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase Rsp5 to membrane proteins in vivo and in vitro. Mol. Biol. Cell 18, 2429–2440
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2429-2440
    • Sullivan, J.A.1    Lewis, M.J.2    Nikko, E.3    Pelham, H.R.4
  • 66
    • 77955058247 scopus 로고    scopus 로고
    • Arrestin domain-containing protein 3 recruits the nedd4 e3 ligase to mediate ubiquitination of the 2-adrenergic receptor
    • Nabhan, J. F., Pan, H., and Lu, Q. (2010) Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase to mediate ubiquitination of the 2-adrenergic receptor. EMBO Rep. 11, 605– 611
    • (2010) EMBO Rep , vol.11 , pp. 605-611
    • Nabhan, J.F.1    Pan, H.2    Lu, Q.3
  • 67
    • 84879049031 scopus 로고    scopus 로고
    • The art-rsp5 ubiquitin ligase network comprises a plasma membrane quality control system that protects yeast cells from proteotoxic stress
    • Zhao, Y., Macgurn, J. A., Liu, M., and Emr, S. (2013) The ART-Rsp5 ubiquitin ligase network comprises a plasma membrane quality control system that protects yeast cells from proteotoxic stress. Elife 2, e00459
    • (2013) Elife , vol.2 , pp. e00459
    • Zhao, Y.1    Macgurn, J.A.2    Liu, M.3    Emr, S.4
  • 68
    • 84951161029 scopus 로고    scopus 로고
    • The α-arrestin arrdc3 mediates alix ubiquitination and g protein-coupled receptor lysosomal sorting
    • Dores, M. R., Lin, H., J. Grimsey, N., Mendez, F., and Trejo, J. (2015) The -arrestin ARRDC3 mediates ALIX ubiquitination and G protein-coupled receptor lysosomal sorting. Mol. Biol. Cell 26, 4660 – 4673
    • (2015) Mol. Biol. Cell , vol.26 , pp. 4660-4673
    • Dores, M.R.1    Lin, H.J.2    Grimsey, N.3    Mendez, F.4    Trejo, J.5
  • 70
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., McCormack, A. L., and Yates, J. R. (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976 –989
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 71
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (lc/lc-ms/ms) for large-scale protein analysis: the yeast proteome
    • Peng, J., Elias, J. E., Thoreen, C. C., Licklider, L. J., and Gygi, S. P. (2003) Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2, 43–50
    • (2003) J. Proteome Res , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 72
    • 0036393898 scopus 로고    scopus 로고
    • Dtaselect and contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L., McDonald, W. H., and Yates, J. R., 3rd. (2002) DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 1, 21–26
    • (2002) J. Proteome Res , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.