메뉴 건너뛰기




Volumn 7, Issue , 2018, Pages

Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; GOLG/ ENDOSOME LOCALIZED DSC PROTEIN 1; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; SIGNAL PEPTIDE; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; VACUOLE LOCAL DSC PROTEIN 1;

EID: 85042094274     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.33116     Document Type: Article
Times cited : (19)

References (62)
  • 1
    • 0036843023 scopus 로고    scopus 로고
    • Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems
    • PMID: 12383343
    • Arvan P, Zhao X, Ramos-Castaneda J, Chang A. 2002. Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems. Traffic 3:771–780. DOI: https://doi.org/10.1034/j.1600-0854.2002.31102.x, PMID: 12383343
    • (2002) Traffic , vol.3 , pp. 771-780
    • Arvan, P.1    Zhao, X.2    Ramos-Castaneda, J.3    Chang, A.4
  • 2
    • 84901675787 scopus 로고    scopus 로고
    • Quality control: Quality control at the plasma membrane: One mechanism does not fit all
    • PMID: 24733583
    • Babst M. 2014. Quality control: quality control at the plasma membrane: one mechanism does not fit all. The Journal of Cell Biology 205:11–20. DOI: https://doi.org/10.1083/jcb.201310113, PMID: 24733583
    • (2014) The Journal of Cell Biology , vol.205 , pp. 11-20
    • Babst, M.1
  • 3
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • PMID: 12651740
    • Bonifacino JS, Traub LM. 2003. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annual Review of Biochemistry 72:395–447. DOI: https://doi.org/10.1146/annurev.biochem.72.121801.161800, PMID: 12651740
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 4
    • 20544447129 scopus 로고    scopus 로고
    • Protein transport from the late Golgi to the vacuole in the yeast Saccharomyces cerevisiae
    • PMID: 15913810
    • Bowers K, Stevens TH. 2005. Protein transport from the late Golgi to the vacuole in the yeast Saccharomyces cerevisiae. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1744:438–454. DOI: https://doi.org/10.1016/j.bbamcr.2005.04.004, PMID: 15913810
    • (2005) Biochimica Et Biophysica Acta (BBA) - Molecular Cell Research , vol.1744 , pp. 438-454
    • Bowers, K.1    Stevens, T.H.2
  • 5
    • 84891658400 scopus 로고    scopus 로고
    • Retromer: A master conductor of endosome sorting
    • PMID: 24492709
    • Burd C, Cullen PJ. 2014. Retromer: a master conductor of endosome sorting. Cold Spring Harbor Perspectives in Biology 6:a016774. DOI: https://doi.org/10.1101/cshperspect.a016774, PMID: 24492709
    • (2014) Cold Spring Harbor Perspectives in Biology , vol.6
    • Burd, C.1    Cullen, P.J.2
  • 6
    • 85030033998 scopus 로고    scopus 로고
    • Dsc E3 ligase localization to the Golgi requires the ATPase Cdc48 and cofactor Ufd1 for activation of sterol regulatory element-binding protein in fission yeast
    • PMID: 28821619
    • Burr R, Ribbens D, Raychaudhuri S, Stewart EV, Ho J, Espenshade PJ. 2017. Dsc E3 ligase localization to the Golgi requires the ATPase Cdc48 and cofactor Ufd1 for activation of sterol regulatory element-binding protein in fission yeast. Journal of Biological Chemistry 292:16333–16350. DOI: https://doi.org/10.1074/jbc.M117.802025, PMID: 28821619
    • (2017) Journal of Biological Chemistry , vol.292 , pp. 16333-16350
    • Burr, R.1    Ribbens, D.2    Raychaudhuri, S.3    Stewart, E.V.4    Ho, J.5    Espenshade, P.J.6
  • 8
    • 0030886261 scopus 로고    scopus 로고
    • The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole
    • PMID: 9335339
    • Cowles CR, Odorizzi G, Payne GS, Emr SD. 1997. The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole. Cell 91:109–118. DOI: https://doi.org/10.1016/S0092-8674(01)80013-1, PMID: 9335339
    • (1997) Cell , vol.91 , pp. 109-118
    • Cowles, C.R.1    Odorizzi, G.2    Payne, G.S.3    Emr, S.D.4
  • 10
    • 84942826638 scopus 로고    scopus 로고
    • Starvation-dependent regulation of golgi quality control links the TOR signaling and vacuolar protein sorting pathways
    • PMID: 26344761
    • Dobzinski N, Chuartzman SG, Kama R, Schuldiner M, Gerst JE. 2015. Starvation-dependent regulation of golgi quality control links the TOR signaling and vacuolar protein sorting pathways. Cell Reports 12:1876–1886. DOI: https://doi.org/10.1016/j.celrep.2015.08.026, PMID: 26344761
    • (2015) Cell Reports , vol.12 , pp. 1876-1886
    • Dobzinski, N.1    Chuartzman, S.G.2    Kama, R.3    Schuldiner, M.4    Gerst, J.E.5
  • 11
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • PMID: 12612637
    • Ellgaard L, Helenius A. 2003. Quality control in the endoplasmic reticulum. Nature Reviews Molecular Cell Biology 4:181–191. DOI: https://doi.org/10.1038/nrm1052, PMID: 12612637
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 12
    • 0037267232 scopus 로고    scopus 로고
    • The role of individual Nedd4-2 (KIAA0439) WW domains in binding and regulating epithelial sodium channels
    • PMID: 12424229
    • Fotia AB, Dinudom A, Shearwin KE, Koch JP, Korbmacher C, Cook DI, Kumar S. 2003. The role of individual Nedd4-2 (KIAA0439) WW domains in binding and regulating epithelial sodium channels. The FASEB Journal 17:70–72. DOI: https://doi.org/10.1096/fj.02-0497fje, PMID: 12424229
    • (2003) The FASEB Journal , vol.17 , pp. 70-72
    • Fotia, A.B.1    Dinudom, A.2    Shearwin, K.E.3    Koch, J.P.4    Korbmacher, C.5    Cook, D.I.6    Kumar, S.7
  • 13
    • 32944455458 scopus 로고    scopus 로고
    • MARCH-III Is a novel component of endosomes with properties similar to those of MARCH-II
    • PMID: 16428329
    • Fukuda H, Nakamura N, Hirose S. 2006. MARCH-III Is a novel component of endosomes with properties similar to those of MARCH-II. The Journal of Biochemistry 139:137–145. DOI: https://doi.org/10.1093/jb/mvj012 PMID: 16428329
    • (2006) The Journal of Biochemistry , vol.139 , pp. 137-145
    • Fukuda, H.1    Nakamura, N.2    Hirose, S.3
  • 14
    • 63449102513 scopus 로고    scopus 로고
    • The LDL receptor. Arteriosclerosis
    • PMID: 19299327
    • Goldstein JL, Brown MS. 2009. The LDL receptor. Arteriosclerosis, Thrombosis, and Vascular Biology 29:431–438. DOI: https://doi.org/10.1161/ATVBAHA.108.179564, PMID: 19299327
    • (2009) Thrombosis, and Vascular Biology , vol.29 , pp. 431-438
    • Goldstein, J.L.1    Brown, M.S.2
  • 15
    • 52049084405 scopus 로고    scopus 로고
    • The anchor-away technique: Rapid, conditional establishment of yeast mutant phenotypes
    • PMID: 1 8922474
    • Haruki H, Nishikawa J, Laemmli UK. 2008. The anchor-away technique: rapid, conditional establishment of yeast mutant phenotypes. Molecular Cell 31:925–932. DOI: https://doi.org/10.1016/j.molcel.2008.07.020, PMID: 1 8922474
    • (2008) Molecular Cell , vol.31 , pp. 925-932
    • Haruki, H.1    Nishikawa, J.2    Laemmli, U.K.3
  • 16
    • 0037415752 scopus 로고    scopus 로고
    • Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval pathways from yeast endosomes
    • PMID: 12554655
    • Hettema EH, Lewis MJ, Black MW, Pelham HR. 2003. Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval pathways from yeast endosomes. The EMBO Journal 22:548–557. DOI: https://doi.org/10.1093/emboj/cdg062, PMID: 12554655
    • (2003) The EMBO Journal , vol.22 , pp. 548-557
    • Hettema, E.H.1    Lewis, M.J.2    Black, M.W.3    Pelham, H.R.4
  • 17
    • 1942439642 scopus 로고    scopus 로고
    • Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins
    • PMID: 14988731
    • Hettema EH, Valdez-Taubas J, Pelham HR. 2004. Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins. The EMBO Journal 23:1279–1288. DOI: https://doi.org/10.1038/sj.emboj.7600137, PMID: 14988731
    • (2004) The EMBO Journal , vol.23 , pp. 1279-1288
    • Hettema, E.H.1    Valdez-Taubas, J.2    Pelham, H.R.3
  • 18
    • 79551550373 scopus 로고    scopus 로고
    • Phylogenetic comparison of F-Box (FBX) gene superfamily within the plant kingdom reveals divergent evolutionary histories indicative of genomic drift
    • PMID: 21297981
    • Hua Z, Zou C, Shiu SH, Vierstra RD. 2011. Phylogenetic comparison of F-Box (FBX) gene superfamily within the plant kingdom reveals divergent evolutionary histories indicative of genomic drift. PLoS One 6:e16219. DOI: https://doi.org/10.1371/journal.pone.0016219, PMID: 21297981
    • (2011) Plos One , vol.6
    • Hua, Z.1    Zou, C.2    Shiu, S.H.3    Vierstra, R.D.4
  • 19
    • 22744456248 scopus 로고    scopus 로고
    • The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme
    • PMID: 15933713
    • Kee Y, Lyon N, Huibregtse JM. 2005. The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme. The EMBO Journal 24:2414–2424. DOI: https://doi.org/10.1038/sj.emboj.7600710, PMID: 15933713
    • (2005) The EMBO Journal , vol.24 , pp. 2414-2424
    • Kee, Y.1    Lyon, N.2    Huibregtse, J.M.3
  • 20
    • 33845970909 scopus 로고    scopus 로고
    • The deubiquitinating enzyme Ubp2 modulates Rsp5-dependent Lys63-linked polyubiquitin conjugates in Saccharomyces cerevisiae
    • PMID: 17028178
    • Kee Y, Muñoz W, Lyon N, Huibregtse JM. 2006. The deubiquitinating enzyme Ubp2 modulates Rsp5-dependent Lys63-linked polyubiquitin conjugates in Saccharomyces cerevisiae. Journal of Biological Chemistry 281:36724–36731. DOI: https://doi.org/10.1074/jbc.M608756200, PMID: 17028178
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 36724-36731
    • Kee, Y.1    Muñoz, W.2    Lyon, N.3    Huibregtse, J.M.4
  • 21
    • 0038349948 scopus 로고    scopus 로고
    • Sequencing and comparison of yeast species to identify genes and regulatory elements
    • PMID: 12748633
    • Kellis M, Patterson N, Endrizzi M, Birren B, Lander ES. 2003. Sequencing and comparison of yeast species to identify genes and regulatory elements. Nature 423:241–254. DOI: https://doi.org/10.1038/nature01644, PMID: 12748633
    • (2003) Nature , vol.423 , pp. 241-254
    • Kellis, M.1    Patterson, N.2    Endrizzi, M.3    Birren, B.4    Lander, E.S.5
  • 23
    • 33746690468 scopus 로고    scopus 로고
    • The F-box protein family
    • PMID: 11178263
    • Kipreos ET, Pagano M. 2000. The F-box protein family. Genome Biology 1:REVIEWS3002. DOI: https://doi.org/10.1186/gb-2000-1-5-reviews3002, PMID: 11178263
    • (2000) Genome Biology 1:REVIEWS3002
    • Kipreos, E.T.1    Pagano, M.2
  • 24
    • 47649106879 scopus 로고    scopus 로고
    • Ear1p and Ssh4p are new adaptors of the ubiquitin ligase Rsp5p for cargo ubiquitylation and sorting at multivesicular bodies
    • PMID: 18367543
    • Léon S, Erpapazoglou Z, Haguenauer-Tsapis R. 2008. Ear1p and Ssh4p are new adaptors of the ubiquitin ligase Rsp5p for cargo ubiquitylation and sorting at multivesicular bodies. Molecular Biology of the Cell 19:2379–2388. DOI: https://doi.org/10.1091/mbc.E08-01-0068, PMID: 18367543
    • (2008) Molecular Biology of the Cell , vol.19 , pp. 2379-2388
    • Léon, S.1    Erpapazoglou, Z.2    Haguenauer-Tsapis, R.3
  • 25
    • 84980349624 scopus 로고    scopus 로고
    • Membrane-anchored ubiquitin ligase complex is required for the turnover of lysosomal membrane proteins
    • PMID: 26527740
    • Li M, Koshi T, Emr SD. 2015a. Membrane-anchored ubiquitin ligase complex is required for the turnover of lysosomal membrane proteins. The Journal of Cell Biology 211:639–652. DOI: https://doi.org/10.1083/jcb.201505062, PMID: 26527740
    • (2015) The Journal of Cell Biology , vol.211 , pp. 639-652
    • Li, M.1    Koshi, T.2    Emr, S.D.3
  • 26
    • 84924915240 scopus 로고    scopus 로고
    • Ubiquitin-dependent lysosomal membrane protein sorting and degradation
    • PMID: 25620559
    • Li M, Rong Y, Chuang YS, Peng D, Emr SD. 2015b. Ubiquitin-dependent lysosomal membrane protein sorting and degradation. Molecular Cell 57:467–478. DOI: https://doi.org/10.1016/j.molcel.2014.12.012, PMID: 25620559
    • (2015) Molecular Cell , vol.57 , pp. 467-478
    • Li, M.1    Rong, Y.2    Chuang, Y.S.3    Peng, D.4    Emr, S.D.5
  • 27
    • 55549102963 scopus 로고    scopus 로고
    • Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface
    • PMID: 18976803
    • Lin CH, MacGurn JA, Chu T, Stefan CJ, Emr SD. 2008. Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135:714–725. DOI: https://doi.org/10.1016/j.cell.2008.09.025, PMID: 18976803
    • (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
  • 28
    • 84947460196 scopus 로고    scopus 로고
    • The AP-3 adaptor complex mediates sorting of yeast and mammalian PQ- loop-family basic amino acid transporters to the vacuolar/lysosomal membrane
    • PMID: 26577948
    • Llinares E, Barry AO, André B. 2015. The AP-3 adaptor complex mediates sorting of yeast and mammalian PQ- loop-family basic amino acid transporters to the vacuolar/lysosomal membrane. Scientific Reports 5:16665. DOI: https://doi.org/10.1038/srep16665, PMID: 26577948
    • (2015) Scientific Reports , vol.5 , pp. 16665
    • Llinares, E.1    Barry, A.O.2    Ré, B.3
  • 30
    • 84861867814 scopus 로고    scopus 로고
    • Ubiquitin and membrane protein turnover: From cradle to grave
    • PMID: 22404628
    • MacGurn JA, Hsu PC, Emr SD. 2012. Ubiquitin and membrane protein turnover: from cradle to grave. Annual Review of Biochemistry 81:231–259. DOI: https://doi.org/10.1146/annurev-biochem-060210-093619, PMID: 22404628
    • (2012) Annual Review of Biochemistry , vol.81 , pp. 231-259
    • Macgurn, J.A.1    Hsu, P.C.2    Emr, S.D.3
  • 33
    • 84983036767 scopus 로고    scopus 로고
    • Types of ubiquitin ligases
    • PMID: 27015313
    • Morreale FE, Walden H. 2016. Types of ubiquitin ligases. Cell 165:248–248.e1. DOI: https://doi.org/10.1016/j.cell.2016.03.003, PMID: 27015313
    • (2016) Cell , vol.165
    • Morreale, F.E.1    Walden, H.2
  • 34
    • 16344381891 scopus 로고    scopus 로고
    • MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking
    • PMID: 15689499
    • Nakamura N, Fukuda H, Kato A, Hirose S. 2005. MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking. Molecular Biology of the Cell 16:1696–1710. DOI: https://doi.org/10.1091/mbc.E04-03-0216, PMID: 15689499
    • (2005) Molecular Biology of the Cell , vol.16 , pp. 1696-1710
    • Nakamura, N.1    Fukuda, H.2    Kato, A.3    Hirose, S.4
  • 35
    • 84055199966 scopus 로고    scopus 로고
    • The role of the transmembrane ring finger proteins in cellular and organelle function
    • PMID: 24957874
    • Nakamura N. 2011. The role of the transmembrane ring finger proteins in cellular and organelle function. Membranes 1:354–393. DOI: https://doi.org/10.3390/membranes1040354, PMID: 24957874
    • (2011) Membranes , vol.1 , pp. 354-393
    • Nakamura, N.1
  • 36
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • PMID: 19029340
    • Narendra D, Tanaka A, Suen DF, Youle RJ. 2008. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. The Journal of Cell Biology 183:795–803. DOI: https://doi.org/10.1083/jcb.200809125, PMID: 19029340
    • (2008) The Journal of Cell Biology , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 37
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • PMID: 9865702
    • Odorizzi G, Babst M, Emr SD. 1998a. Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Cell 95:847–858. DOI: https://doi.org/10.1016/S0092-8674(00)81707-9, PMID: 9865702
    • (1998) Cell , vol.95 , pp. 847-858
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 38
    • 0032404443 scopus 로고    scopus 로고
    • The AP-3 complex: A coat of many colours
    • PMID: 9714600
    • Odorizzi G, Cowles CR, Emr SD. 1998b. The AP-3 complex: a coat of many colours. Trends in Cell Biology 8: 282–288. DOI: https://doi.org/10.1016/S0962-8924(98)01295-1, PMID: 9714600
    • (1998) Trends in Cell Biology , vol.8 , pp. 282-288
    • Odorizzi, G.1    Cowles, C.R.2    Emr, S.D.3
  • 39
    • 77955607650 scopus 로고    scopus 로고
    • Peripheral protein quality control removes unfolded CFTR from the plasma membrane
    • PMID: 20595578
    • Okiyoneda T, Barrière H, Bagdány M, Rabeh WM, Du K, Höhfeld J, Young JC, Lukacs GL. 2010. Peripheral protein quality control removes unfolded CFTR from the plasma membrane. Science 329:805–810. DOI: https://doi.org/10.1126/science.1191542, PMID: 20595578
    • (2010) Science , vol.329 , pp. 805-810
    • Okiyoneda, T.1    Barrière, H.2    Bagdány, M.3    Rabeh, W.M.4    Du, K.5    Höhfeld, J.6    Young, J.C.7    Lukacs, G.L.8
  • 40
  • 41
    • 0036166924 scopus 로고    scopus 로고
    • A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies
    • PMID: 11788821
    • Reggiori F, Pelham HR. 2002. A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies. Nature Cell Biology 4:117–123. DOI: https://doi.org/10.1038/ncb743, PMID: 11788821
    • (2002) Nature Cell Biology , vol.4 , pp. 117-123
    • Reggiori, F.1    Pelham, H.R.2
  • 42
    • 76249107656 scopus 로고    scopus 로고
    • Rapid inactivation of proteins by rapamycin-induced rerouting to mitochondria
    • PMID: 2015 9602
    • Robinson MS, Sahlender DA, Foster SD. 2010. Rapid inactivation of proteins by rapamycin-induced rerouting to mitochondria. Developmental Cell 18:324–331. DOI: https://doi.org/10.1016/j.devcel.2009.12.015, PMID: 2015 9602
    • (2010) Developmental Cell , vol.18 , pp. 324-331
    • Robinson, M.S.1    Sahlender, D.A.2    Foster, S.D.3
  • 43
    • 84896270715 scopus 로고    scopus 로고
    • Quality control: ER-associated degradation: Protein quality control and beyond
    • PMID: 24637321
    • Ruggiano A, Foresti O, Carvalho P. 2014. Quality control: ER-associated degradation: protein quality control and beyond. The Journal of Cell Biology 204:869–879. DOI: https://doi.org/10.1083/jcb.201312042, PMID: 24637321
    • (2014) The Journal of Cell Biology , vol.204 , pp. 869-879
    • Ruggiano, A.1    Foresti, O.2    Carvalho, P.3
  • 44
    • 0030897485 scopus 로고    scopus 로고
    • Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene products
    • PMID: 9105038
    • Seaman MN, Marcusson EG, Cereghino JL, Emr SD. 1997. Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene products. The Journal of Cell Biology 137:79–92. DOI: https://doi.org/10.1083/jcb.137.1.79, PMID: 9105038
    • (1997) The Journal of Cell Biology , vol.137 , pp. 79-92
    • Seaman, M.N.1    Marcusson, E.G.2    Cereghino, J.L.3    Emr, S.D.4
  • 45
    • 84930733719 scopus 로고    scopus 로고
    • Loss of ATP- dependent lysine uptake in the vacuolar membrane vesicles of Saccharomyces cerevisiae ypq1D mutant. Bioscience
    • PMID: 25229858
    • Sekito T, Nakamura K, Manabe K, Tone J, Sato Y, Murao N, Kawano-Kawada M, Kakinuma Y. 2014. Loss of ATP- dependent lysine uptake in the vacuolar membrane vesicles of Saccharomyces cerevisiae ypq1D mutant. Bioscience, Biotechnology, and Biochemistry 78:1199–1202. DOI: https://doi.org/10.1080/09168451.2014.918489, PMID: 25229858
    • (2014) Biotechnology, and Biochemistry , vol.78 , pp. 1199-1202
    • Sekito, T.1    Nakamura, K.2    Manabe, K.3    Tone, J.4    Sato, Y.5    Murao, N.6    Kawano-Kawada, M.7    Kakinuma, Y.8
  • 48
    • 84855288996 scopus 로고    scopus 로고
    • Yeast sterol regulatory element-binding protein (SREBP) cleavage requires Cdc48 and Dsc5, a ubiquitin regulatory X domain-containing subunit of the Golgi Dsc E3 ligase
    • PMID: 22086920
    • Stewart EV, Lloyd SJ, Burg JS, Nwosu CC, Lintner RE, Daza R, Russ C, Ponchner K, Nusbaum C, Espenshade PJ. 2012. Yeast sterol regulatory element-binding protein (SREBP) cleavage requires Cdc48 and Dsc5, a ubiquitin regulatory X domain-containing subunit of the Golgi Dsc E3 ligase. Journal of Biological Chemistry 287:672–681. DOI: https://doi.org/10.1074/jbc.M111.317370, PMID: 22086920
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 672-681
    • Stewart, E.V.1    Lloyd, S.J.2    Burg, J.S.3    Nwosu, C.C.4    Lintner, R.E.5    Daza, R.6    Russ, C.7    Ponchner, K.8    Nusbaum, C.9    Espenshade, P.J.10
  • 50
    • 34247143246 scopus 로고    scopus 로고
    • Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling
    • PMID: 17420293
    • Strochlic TI, Setty TG, Sitaram A, Burd CG. 2007. Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling. The Journal of Cell Biology 177:115–125. DOI: https://doi.org/10.1083/jcb.200609161, PMID: 17420293
    • (2007) The Journal of Cell Biology , vol.177 , pp. 115-125
    • Strochlic, T.I.1    Setty, T.G.2    Sitaram, A.3    Burd, C.G.4
  • 51
    • 84925593828 scopus 로고    scopus 로고
    • The RING finger E3 ligase STRF1 is involved in membrane trafficking and modulates salt-stress response in Arabidopsis thaliana
    • PMID: 25704231
    • Tian M, Lou L, Liu L, Yu F, Zhao Q, Zhang H, Wu Y, Tang S, Xia R, Zhu B, Serino G, Xie Q. 2015. The RING finger E3 ligase STRF1 is involved in membrane trafficking and modulates salt-stress response in Arabidopsis thaliana. The Plant Journal 82:81–92. DOI: https://doi.org/10.1111/tpj.12797, PMID: 25704231
    • (2015) The Plant Journal , vol.82 , pp. 81-92
    • Tian, M.1    Lou, L.2    Liu, L.3    Yu, F.4    Zhao, Q.5    Zhang, H.6    Wu, Y.7    Tang, S.8    Xia, R.9    Zhu, B.10    Serino, G.11    Xie, Q.12
  • 52
    • 84910673082 scopus 로고    scopus 로고
    • Identification of candidate substrates for the Golgi Tul1 E3 ligase using quantitative diGly proteomics in yeast
    • PMID: 25078903
    • Tong Z, Kim MS, Pandey A, Espenshade PJ. 2014. Identification of candidate substrates for the Golgi Tul1 E3 ligase using quantitative diGly proteomics in yeast. Molecular & Cellular Proteomics 13:2871–2882. DOI: https://doi.org/10.1074/mcp.M114.040774, PMID: 25078903
    • (2014) Molecular & Cellular Proteomics , vol.13 , pp. 2871-2882
    • Tong, Z.1    Kim, M.S.2    Pandey, A.3    Espenshade, P.J.4
  • 53
    • 84979862598 scopus 로고    scopus 로고
    • The topcons web server for consensus prediction of membrane protein topology and signal peptides
    • PMID: 25969446
    • Tsirigos KD, Peters C, Shu N, Käll L, Elofsson A. 2015. The topcons web server for consensus prediction of membrane protein topology and signal peptides. Nucleic Acids Research 43:W401–W407. DOI: https://doi.org/10.1093/nar/gkv485, PMID: 25969446
    • (2015) Nucleic Acids Research , vol.43 , pp. W401-W407
    • Tsirigos, K.D.1    Peters, C.2    Shu, N.3    Käll, L.4    Elofsson, A.5
  • 54
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • PMID: 7533169
    • Vida TA, Emr SD. 1995. A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. The Journal of Cell Biology 128:779–792. DOI: https://doi.org/10.1083/jcb.128.5.779, PMID: 7533169
    • (1995) The Journal of Cell Biology , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 55
    • 84876755289 scopus 로고    scopus 로고
    • Flying saucer1 is a transmembrane RING E3 ubiquitin ligase that regulates the degree of pectin methylesterification in Arabidopsis seed mucilage
    • PMID: 23482858
    • Voiniciuc C, Dean GH, Griffiths JS, Kirchsteiger K, Hwang YT, Gillett A, Dow G, Western TL, Estelle M, Haughn GW. 2013. Flying saucer1 is a transmembrane RING E3 ubiquitin ligase that regulates the degree of pectin methylesterification in Arabidopsis seed mucilage. The Plant Cell 25:944–959. DOI: https://doi.org/10.1105/tpc.112.107888, PMID: 23482858
    • (2013) The Plant Cell , vol.25 , pp. 944-959
    • Voiniciuc, C.1    Dean, G.H.2    Griffiths, J.S.3    Kirchsteiger, K.4    Hwang, Y.T.5    Gillett, A.6    Dow, G.7    Western, T.L.8    Estelle, M.9    Haughn, G.W.10
  • 56
    • 0035032224 scopus 로고    scopus 로고
    • Localization of the Rsp5p ubiquitin-protein ligase at multiple sites within the endocytic pathway
    • PMID: 11313482
    • Wang G, McCaffery JM, Wendland B, Dupré S, Haguenauer-Tsapis R, Huibregtse JM. 2001. Localization of the Rsp5p ubiquitin-protein ligase at multiple sites within the endocytic pathway. Molecular and Cellular Biology 21:3564–3575. DOI: https://doi.org/10.1128/MCB.21.10.3564-3575.2001, PMID: 11313482
    • (2001) Molecular and Cellular Biology , vol.21 , pp. 3564-3575
    • Wang, G.1    McCaffery, J.M.2    Wendland, B.3    Dupré, S.4    Haguenauer-Tsapis, R.5    Huibregtse, J.M.6
  • 57
    • 80051681133 scopus 로고    scopus 로고
    • Routing misfolded proteins through the multivesicular body (MVB) pathway protects against proteotoxicity
    • PMID: 21708947
    • Wang S, Thibault G, Ng DT. 2011. Routing misfolded proteins through the multivesicular body (MVB) pathway protects against proteotoxicity. Journal of Biological Chemistry 286:29376–29387. DOI: https://doi.org/10.1074/jbc.M111.233346, PMID: 21708947
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 29376-29387
    • Wang, S.1    Thibault, G.2    Ng, D.T.3
  • 59
    • 49449096720 scopus 로고    scopus 로고
    • Pex10p functions as an E3 ligase for the Ubc4p-dependent ubiquitination of Pex5p
    • PMID: 18644345
    • Williams C, van den Berg M, Geers E, Distel B. 2008. Pex10p functions as an E3 ligase for the Ubc4p-dependent ubiquitination of Pex5p. Biochemical and Biophysical Research Communications 374:620–624. DOI: https://doi.org/10.1016/j.bbrc.2008.07.054, PMID: 18644345
    • (2008) Biochemical and Biophysical Research Communications , vol.374 , pp. 620-624
    • Williams, C.1    Van Den Berg, M.2    Geers, E.3    Distel, B.4
  • 61
    • 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
    • PMID: 23599894
    • Zhao Y, Macgurn JA, Liu M, 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. DOI: https://doi.org/10.7554/eLife.00459, PMID: 23599894
    • (2013) Elife , vol.2
    • Zhao, Y.1    Macgurn, J.A.2    Liu, M.3    Emr, S.4
  • 62
    • 85027172280 scopus 로고    scopus 로고
    • ESCRTs function directly on the lysosome membrane to downregulate ubiquitinated lysosomal membrane proteins
    • PMID: 28661397
    • Zhu L, Jorgensen JR, Li M, Chuang YS, Emr SD. 2017. ESCRTs function directly on the lysosome membrane to downregulate ubiquitinated lysosomal membrane proteins. eLife 6:e26403. DOI: https://doi.org/10.7554/eLife.26403, PMID: 28661397
    • (2017) Elife , vol.6
    • Zhu, L.1    Jorgensen, J.R.2    Li, M.3    Chuang, Y.S.4    Emr, S.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.