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Volumn 20, Issue 4, 2010, Pages 196-204

The ubiquitin code of yeast permease trafficking

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL ENZYME; GENERAL AMINO ACID PERMEASE; NITROGEN PERMEASE INACTIVATOR PROTEIN; PERMEASE; PROTEIN ARN1; PROTEIN FUR4; PROTEIN RSP5; PROTEIN SIT1; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 77950857969     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2010.01.004     Document Type: Review
Times cited : (207)

References (103)
  • 2
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D., Kumar S. Physiological functions of the HECT family of ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 2009, 10:398-409.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 3
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih S.C., et al. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat. Cell Biol. 2002, 4:389-393.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 389-393
    • Shih, S.C.1
  • 4
    • 33750555919 scopus 로고    scopus 로고
    • Ubiquitin-binding domains
    • Hurley J.H., et al. Ubiquitin-binding domains. Biochem. J. 2006, 399:361-372.
    • (2006) Biochem. J. , vol.399 , pp. 361-372
    • Hurley, J.H.1
  • 5
    • 33646147146 scopus 로고    scopus 로고
    • Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules
    • Duncan L.M., et al. Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules. EMBO J. 2006, 25:1635-1645.
    • (2006) EMBO J. , vol.25 , pp. 1635-1645
    • Duncan, L.M.1
  • 6
    • 34347401218 scopus 로고    scopus 로고
    • Regulation of receptors and transporters by ubiquitination: new insights into surprisingly similar mechanisms
    • Miranda M., Sorkin A. Regulation of receptors and transporters by ubiquitination: new insights into surprisingly similar mechanisms. Mol. Interv. 2007, 7:157-167.
    • (2007) Mol. Interv. , vol.7 , pp. 157-167
    • Miranda, M.1    Sorkin, A.2
  • 7
    • 70350376635 scopus 로고    scopus 로고
    • Internalization and intracellular sorting of the EGF receptor: a model for understanding the mechanisms of receptor trafficking
    • Madshus I.H., Stang E. Internalization and intracellular sorting of the EGF receptor: a model for understanding the mechanisms of receptor trafficking. J. Cell Sci. 2009, 122:3433-3439.
    • (2009) J. Cell Sci. , vol.122 , pp. 3433-3439
    • Madshus, I.H.1    Stang, E.2
  • 8
    • 39149132089 scopus 로고    scopus 로고
    • ESCRT complexes and the biogenesis of multivesicular bodies
    • Hurley J.H. ESCRT complexes and the biogenesis of multivesicular bodies. Curr. Opin. Cell Biol. 2008, 20:4-11.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 4-11
    • Hurley, J.H.1
  • 9
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated proteins
    • Raiborg C., Stenmark H. The ESCRT machinery in endosomal sorting of ubiquitylated proteins. Nature 2009, 458:445-452.
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 10
    • 65349101661 scopus 로고    scopus 로고
    • ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting
    • Shields S.B., et al. ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting. J. Cell Biol. 2009, 185:213-224.
    • (2009) J. Cell Biol. , vol.185 , pp. 213-224
    • Shields, S.B.1
  • 11
    • 65349190586 scopus 로고    scopus 로고
    • The circuitry of cargo flux in the ESCRT pathway
    • Hurley J.H., Ren X. The circuitry of cargo flux in the ESCRT pathway. J. Cell Biol. 2009, 185:185-187.
    • (2009) J. Cell Biol. , vol.185 , pp. 185-187
    • Hurley, J.H.1    Ren, X.2
  • 12
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kölling R., Hollenberg C.P. The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J. 1994, 13:3261-3271.
    • (1994) EMBO J. , vol.13 , pp. 3261-3271
    • Kölling, R.1    Hollenberg, C.P.2
  • 13
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke L., Riezman H. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 1996, 84:277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 14
    • 0020774482 scopus 로고
    • Inactivation-reactivation process and repression of permease formation regulate several ammonia-sensitive permeases in the yeast Saccharomyces cerevisiae
    • Grenson M. Inactivation-reactivation process and repression of permease formation regulate several ammonia-sensitive permeases in the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 1983, 133:135-139.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 135-139
    • Grenson, M.1
  • 15
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse J.M., et al. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:2563-2567.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1
  • 16
    • 0028971506 scopus 로고
    • NPI1, an essential gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein C., et al. NPI1, an essential gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol. Microbiol. 1995, 18:77-87.
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1
  • 17
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan J.-M., et al. Ubiquitination mediated by the Npi1/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem. 1996, 271:10946-10952.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.-M.1
  • 18
    • 65449183853 scopus 로고    scopus 로고
    • Viral avoidance and exploitation of the ubiquitin system
    • Randow F., Lehner P.J. Viral avoidance and exploitation of the ubiquitin system. Nat. Cell Biol. 2009, 11:527-534.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 527-534
    • Randow, F.1    Lehner, P.J.2
  • 19
    • 33947714944 scopus 로고    scopus 로고
    • Bacterial interference of ubiquitination and deubiquitination
    • Rytkönen A., Holden D.W. Bacterial interference of ubiquitination and deubiquitination. Cell Host Microbe 2007, 1:13-22.
    • (2007) Cell Host Microbe , vol.1 , pp. 13-22
    • Rytkönen, A.1    Holden, D.W.2
  • 20
    • 0034677207 scopus 로고    scopus 로고
    • Monoubiquitin carries a novel internalization signal that is appended to activated receptors
    • Shih S.C., et al. Monoubiquitin carries a novel internalization signal that is appended to activated receptors. EMBO J. 2000, 19:187-198.
    • (2000) EMBO J. , vol.19 , pp. 187-198
    • Shih, S.C.1
  • 21
    • 67649227630 scopus 로고    scopus 로고
    • Polyubiquitination by HECT E3s and the determinants of chain type specificity
    • Kim H.C., Huibregtse J.M. Polyubiquitination by HECT E3s and the determinants of chain type specificity. Mol. Cell. Biol. 2009, 29:3307-3318.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3307-3318
    • Kim, H.C.1    Huibregtse, J.M.2
  • 22
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell J., et al. A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol. Cell 1998, 1:193-202.
    • (1998) Mol. Cell , vol.1 , pp. 193-202
    • Terrell, J.1
  • 23
    • 0343593730 scopus 로고    scopus 로고
    • Monoubiquitination is sufficient to signal internalization of the maltose transporter in Saccharomyces cerevisiae
    • Lucero P., et al. Monoubiquitination is sufficient to signal internalization of the maltose transporter in Saccharomyces cerevisiae. J. Bacteriol. 2000, 182:241-243.
    • (2000) J. Bacteriol. , vol.182 , pp. 241-243
    • Lucero, P.1
  • 24
    • 0033048856 scopus 로고    scopus 로고
    • +-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains
    • +-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains. J. Cell Sci. 1999, 112:1375-1383.
    • (1999) J. Cell Sci. , vol.112 , pp. 1375-1383
    • Springael, J.-Y.1
  • 25
    • 65649128660 scopus 로고    scopus 로고
    • K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway
    • Lauwers E., et al. K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. J. Cell Biol. 2009, 185:493-502.
    • (2009) J. Cell Biol. , vol.185 , pp. 493-502
    • Lauwers, E.1
  • 26
    • 0742288015 scopus 로고    scopus 로고
    • Direct sorting of the yeast uracil permease to the endosomal system is controlled by uracil binding and Rsp5p-dependent ubiquitylation
    • Blondel M.-O., et al. Direct sorting of the yeast uracil permease to the endosomal system is controlled by uracil binding and Rsp5p-dependent ubiquitylation. Mol. Biol. Cell 2004, 15:883-895.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 883-895
    • Blondel, M.-O.1
  • 27
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan J.M., Haguenauer-Tsapis R. Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 1997, 16:5847-5854.
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 28
    • 67749127761 scopus 로고    scopus 로고
    • Glucose-induced ubiquitylation and endocytosis of the yeast JEN1 transporter: role of lysine 63-linked ubiquitin chains
    • Paiva S., et al. Glucose-induced ubiquitylation and endocytosis of the yeast JEN1 transporter: role of lysine 63-linked ubiquitin chains. J. Biol. Chem. 2009, 284:19228-19236.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19228-19236
    • Paiva, S.1
  • 29
    • 33644529627 scopus 로고    scopus 로고
    • Molecular basis of oligoubiquitin-dependent internalization of membrane proteins in mammalian cells
    • Barrière H., et al. Molecular basis of oligoubiquitin-dependent internalization of membrane proteins in mammalian cells. Traffic 2006, 7:282-297.
    • (2006) Traffic , vol.7 , pp. 282-297
    • Barrière, H.1
  • 30
    • 33644502037 scopus 로고    scopus 로고
    • Epsin 1 is a polyubiquitin-selective clathrin-associated sorting protein
    • Hawryluk M.J., et al. Epsin 1 is a polyubiquitin-selective clathrin-associated sorting protein. Traffic 2006, 7:262-281.
    • (2006) Traffic , vol.7 , pp. 262-281
    • Hawryluk, M.J.1
  • 31
    • 69149088033 scopus 로고    scopus 로고
    • Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by tandem UIMs of RAP80
    • Sato Y., et al. Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by tandem UIMs of RAP80. EMBO J. 2009, 28:2461-2468.
    • (2009) EMBO J. , vol.28 , pp. 2461-2468
    • Sato, Y.1
  • 32
    • 68249135262 scopus 로고    scopus 로고
    • Avid interactions underlie the Lys63-linked polyubiquitin binding specificities observed for UBA domains
    • Sims J.J., et al. Avid interactions underlie the Lys63-linked polyubiquitin binding specificities observed for UBA domains. Nat. Struct. Mol. Biol. 2009, 16:883-889.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 883-889
    • Sims, J.J.1
  • 33
    • 0032217156 scopus 로고    scopus 로고
    • C-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor
    • Levkowitz G., et al. c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 1998, 12:3663-3674.
    • (1998) Genes Dev. , vol.12 , pp. 3663-3674
    • Levkowitz, G.1
  • 34
    • 0035173239 scopus 로고    scopus 로고
    • Uptake of the ATP-binding cassette (ABC) transporter Ste6 into the yeast vacuole is blocked in the doa4 mutant
    • Losko S., et al. Uptake of the ATP-binding cassette (ABC) transporter Ste6 into the yeast vacuole is blocked in the doa4 mutant. Mol. Biol. Cell 2001, 12:1047-1059.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1047-1059
    • Losko, S.1
  • 35
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • Odorizzi G., et al. Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Cell 1998, 95:847-858.
    • (1998) Cell , vol.95 , pp. 847-858
    • Odorizzi, G.1
  • 36
    • 0035903635 scopus 로고    scopus 로고
    • Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting
    • Reggiori F., Pelham H.R. Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting. EMBO J. 2001, 20:5176-5186.
    • (2001) EMBO J. , vol.20 , pp. 5176-5186
    • Reggiori, F.1    Pelham, H.R.2
  • 37
    • 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., et al. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 2001, 106:145-155.
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1
  • 38
    • 0034852403 scopus 로고    scopus 로고
    • Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole
    • Urbanowski J.L., Piper R.C. Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole. Traffic 2001, 2:622-630.
    • (2001) Traffic , vol.2 , pp. 622-630
    • Urbanowski, J.L.1    Piper, R.C.2
  • 39
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann D.J., et al. Receptor downregulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 2002, 3:893-905.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 893-905
    • Katzmann, D.J.1
  • 40
    • 47649108312 scopus 로고    scopus 로고
    • Substrate and ubiquitin-dependent trafficking of the yeast siderophore transporter Sit1
    • Erpapazoglou Z., et al. Substrate and ubiquitin-dependent trafficking of the yeast siderophore transporter Sit1. Traffic 2008, 9:1372-1391.
    • (2008) Traffic , vol.9 , pp. 1372-1391
    • Erpapazoglou, Z.1
  • 41
    • 34948905713 scopus 로고    scopus 로고
    • Plasticity of poly-ubiquitin recognition as lysosomal targeting signals by the endosomal sorting machinery
    • Barrière H., et al. Plasticity of poly-ubiquitin recognition as lysosomal targeting signals by the endosomal sorting machinery. Mol. Biol. Cell 2007, 18:3952-3965.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3952-3965
    • Barrière, H.1
  • 42
    • 33644852909 scopus 로고    scopus 로고
    • Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain
    • Huang F., et al. Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol. Cell 2006, 21:737-748.
    • (2006) Mol. Cell , vol.21 , pp. 737-748
    • Huang, F.1
  • 43
    • 33845307572 scopus 로고    scopus 로고
    • Short-chain ubiquitination mediates the regulated endocytosis of the aquaporin-2 water channel
    • Kamsteeg E.J., et al. Short-chain ubiquitination mediates the regulated endocytosis of the aquaporin-2 water channel. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:18344-18349.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 18344-18349
    • Kamsteeg, E.J.1
  • 44
    • 0033588918 scopus 로고    scopus 로고
    • Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast
    • Beck T., et al. Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast. J. Cell Biol. 1999, 146:1227-1238.
    • (1999) J. Cell Biol. , vol.146 , pp. 1227-1238
    • Beck, T.1
  • 45
    • 0035941194 scopus 로고    scopus 로고
    • Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1
    • Soetens O., et al. Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1. J. Biol. Chem. 2001, 276:43949-43957.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43949-43957
    • Soetens, O.1
  • 46
    • 0035858866 scopus 로고    scopus 로고
    • Components of a ubiquitin ligase complex specify polyubiquitylation and intracellular trafficking of the general amino acid permease
    • Helliwell S.B., et al. Components of a ubiquitin ligase complex specify polyubiquitylation and intracellular trafficking of the general amino acid permease. J. Cell Biol. 2001, 153:649-662.
    • (2001) J. Cell Biol. , vol.153 , pp. 649-662
    • Helliwell, S.B.1
  • 47
    • 0038491550 scopus 로고    scopus 로고
    • Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane
    • Umebayashi K., Nakano A. Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane. J. Cell Biol. 2003, 161:1117-1131.
    • (2003) J. Cell Biol. , vol.161 , pp. 1117-1131
    • Umebayashi, K.1    Nakano, A.2
  • 48
    • 51349159616 scopus 로고    scopus 로고
    • Different ubiquitin signals act at the Golgi and plasma membrane to direct GAP1 Trafficking
    • Risinger A.L., Kaiser C.A. Different ubiquitin signals act at the Golgi and plasma membrane to direct GAP1 Trafficking. Mol. Biol. Cell 2008, 19:2962-2972.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2962-2972
    • Risinger, A.L.1    Kaiser, C.A.2
  • 49
    • 11144247939 scopus 로고    scopus 로고
    • The GAT domains of clathrin-associated gga proteins have two ubiquitin binding motifs
    • Bilodeau P.S., et al. The GAT domains of clathrin-associated gga proteins have two ubiquitin binding motifs. J. Biol. Chem. 2004, 279:54808-54816.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54808-54816
    • Bilodeau, P.S.1
  • 50
    • 11144225699 scopus 로고    scopus 로고
    • GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network
    • Scott P.M., et al. GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network. Nat. Cell Biol. 2004, 6:252-259.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 252-259
    • Scott, P.M.1
  • 51
    • 69949152537 scopus 로고    scopus 로고
    • GGA2 mediates sequential ubiquitin-independent and -dependent steps in the trafficking of ARN1 from the trans-golgi network to the vacuole
    • Deng Y., et al. GGA2 mediates sequential ubiquitin-independent and -dependent steps in the trafficking of ARN1 from the trans-golgi network to the vacuole. J. Biol. Chem. 2009, 284:23830-23841.
    • (2009) J. Biol. Chem. , vol.284 , pp. 23830-23841
    • Deng, Y.1
  • 52
    • 34248165966 scopus 로고    scopus 로고
    • GGA2- and ubiquitin-dependent trafficking of Arn1, the ferrichrome transporter of Saccharomyces cerevisiae
    • Kim Y., et al. GGA2- and ubiquitin-dependent trafficking of Arn1, the ferrichrome transporter of Saccharomyces cerevisiae. Mol. Biol. Cell 2007, 18:1790-1802.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1790-1802
    • Kim, Y.1
  • 53
    • 1542714469 scopus 로고    scopus 로고
    • Interactions of GGA3 with the ubiquitin sorting machinery
    • Puertollano R., Bonifacino J.S. Interactions of GGA3 with the ubiquitin sorting machinery. Nat. Cell Biol. 2004, 6:244-251.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 244-251
    • Puertollano, R.1    Bonifacino, J.S.2
  • 54
    • 0027988814 scopus 로고
    • The WW domain: a signalling site in dystrophin?
    • Bork P., Sudol M. The WW domain: a signalling site in dystrophin?. Trends Biochem. Sci. 1994, 19:531-533.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 531-533
    • Bork, P.1    Sudol, M.2
  • 55
    • 0028648838 scopus 로고
    • WWP, a new amino acid motif present in single or multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65
    • André B., Springael J.Y. WWP, a new amino acid motif present in single or multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65. Biochem. Biophys. Res. Commun. 1994, 205:1201-1205.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1201-1205
    • André, B.1    Springael, J.Y.2
  • 56
    • 0029874436 scopus 로고    scopus 로고
    • WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome
    • Staub O., et al. WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome. EMBO J. 1996, 15:2371-2380.
    • (1996) EMBO J. , vol.15 , pp. 2371-2380
    • Staub, O.1
  • 57
    • 33846821642 scopus 로고    scopus 로고
    • Direct binding to Rsp5 mediates ubiquitin-independent sorting of Sna3 via the multivesicular body pathway
    • McNatt M.W., et al. Direct binding to Rsp5 mediates ubiquitin-independent sorting of Sna3 via the multivesicular body pathway. Mol. Biol. Cell 2007, 18:697-706.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 697-706
    • McNatt, M.W.1
  • 58
    • 11144228252 scopus 로고    scopus 로고
    • A single PXY motif located within the carboxyl terminus of Spt23p and Mga2p mediates a physical and functional interaction with ubiquitin ligase Rsp5p
    • Shcherbik N., et al. A single PXY motif located within the carboxyl terminus of Spt23p and Mga2p mediates a physical and functional interaction with ubiquitin ligase Rsp5p. J. Biol. Chem. 2004, 279:53892-53898.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53892-53898
    • Shcherbik, N.1
  • 59
    • 33846807370 scopus 로고    scopus 로고
    • Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5
    • Oestreich A.J., et al. Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Mol. Biol. Cell 2007, 18:707-720.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 707-720
    • Oestreich, A.J.1
  • 60
    • 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., et al. Targeting of Sna3p to the endosomal pathway depends on its interaction with Rsp5p and multivesicular body sorting on its ubiquitylation. Traffic 2007, 8:1280-1296.
    • (2007) Traffic , vol.8 , pp. 1280-1296
    • Stawiecka-Mirota, M.1
  • 61
    • 34248162393 scopus 로고    scopus 로고
    • Direct binding to Rsp5p regulates ubiquitination-independent vacuolar transport of Sna3p
    • Watson H., Bonifacino J.S. Direct binding to Rsp5p regulates ubiquitination-independent vacuolar transport of Sna3p. Mol. Biol. Cell 2007, 18:1781-1789.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1781-1789
    • Watson, H.1    Bonifacino, J.S.2
  • 62
    • 67349113489 scopus 로고    scopus 로고
    • Ubiquitin ligase adaptors: regulators of ubiquitylation and endocytosis of plasma membrane proteins
    • Léon S., Haguenauer-Tsapis R. Ubiquitin ligase adaptors: regulators of ubiquitylation and endocytosis of plasma membrane proteins. Exp. Cell Res. 2009, 315:1574-1583.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1574-1583
    • Léon, S.1    Haguenauer-Tsapis, R.2
  • 63
    • 55549102963 scopus 로고    scopus 로고
    • Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface
    • Lin C.H., et al. Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 2008, 135:714-725.
    • (2008) Cell , vol.135 , pp. 714-725
    • Lin, C.H.1
  • 64
    • 70649112359 scopus 로고    scopus 로고
    • Arrestin-mediated endocytosis of yeast plasma membrane transporters
    • Nikko E., Pelham H.R. Arrestin-mediated endocytosis of yeast plasma membrane transporters. Traffic 2009, 10:1856-1867.
    • (2009) Traffic , vol.10 , pp. 1856-1867
    • Nikko, E.1    Pelham, H.R.2
  • 65
    • 58149158220 scopus 로고    scopus 로고
    • Regulation of the divalent metal ion transporter DMT1 and iron homeostasis by a ubiquitin-dependent mechanism involving Ndfips and WWP2
    • Foot N.J., et al. Regulation of the divalent metal ion transporter DMT1 and iron homeostasis by a ubiquitin-dependent mechanism involving Ndfips and WWP2. Blood 2008, 112:4268-4275.
    • (2008) Blood , vol.112 , pp. 4268-4275
    • Foot, N.J.1
  • 66
    • 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., et al. Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase rsp5 to membrane proteins in vivo and in vitro. Mol. Biol. Cell 2007, 18:2429-2440.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2429-2440
    • Sullivan, J.A.1
  • 67
    • 57049101734 scopus 로고    scopus 로고
    • Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1
    • Nikko E., et al. Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1. EMBO Rep. 2008, 9:1216-1221.
    • (2008) EMBO Rep. , vol.9 , pp. 1216-1221
    • Nikko, E.1
  • 68
    • 0031961993 scopus 로고    scopus 로고
    • A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease
    • Marchal C., et al. A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease. Mol. Cell. Biol. 1998, 18:314-321.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 314-321
    • Marchal, C.1
  • 69
    • 1642356961 scopus 로고    scopus 로고
    • The internalization of yeast Ste6p follows an ordered series of events involving phosphorylation, ubiquitination, recognition and endocytosis
    • Kelm K.B., et al. The internalization of yeast Ste6p follows an ordered series of events involving phosphorylation, ubiquitination, recognition and endocytosis. Traffic 2004, 5:165-180.
    • (2004) Traffic , vol.5 , pp. 165-180
    • Kelm, K.B.1
  • 70
    • 47649106879 scopus 로고    scopus 로고
    • Ear1p and Ssh4p are new adaptors of the ubiquitin ligase Rsp5p for cargo ubiquitylation and sorting at multivesicular bodies
    • Léon S., et al. Ear1p and Ssh4p are new adaptors of the ubiquitin ligase Rsp5p for cargo ubiquitylation and sorting at multivesicular bodies. Mol. Biol. Cell 2008, 19:2379-2388.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2379-2388
    • Léon, S.1
  • 71
    • 33750530169 scopus 로고    scopus 로고
    • Itch/AIP4 mediates Deltex degradation through the formation of K29-linked polyubiquitin chains
    • Chastagner P., Israël A.a.B.C. Itch/AIP4 mediates Deltex degradation through the formation of K29-linked polyubiquitin chains. EMBO Rep. 2006, 7:1147-1153.
    • (2006) EMBO Rep. , vol.7 , pp. 1147-1153
    • Chastagner, P.1    Israël, A.2
  • 72
    • 73549090361 scopus 로고    scopus 로고
    • Efficient internalization of MHC I requires lysine-11 and lysine-63 mixed linkage polyubiquitin chains
    • Boname J.M., et al. Efficient internalization of MHC I requires lysine-11 and lysine-63 mixed linkage polyubiquitin chains. Traffic 2009, 11:210-220.
    • (2009) Traffic , vol.11 , pp. 210-220
    • Boname, J.M.1
  • 73
    • 33750529154 scopus 로고    scopus 로고
    • Working out coupled monoubiquitylation
    • Haglund K., Stenmark H. Working out coupled monoubiquitylation. Nat. Cell Biol. 2006, 8:1218-1219.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1218-1219
    • Haglund, K.1    Stenmark, H.2
  • 74
    • 33646788800 scopus 로고    scopus 로고
    • The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation
    • Row P.E., et al. The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. J. Biol. Chem. 2006, 281:12618-12624.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12618-12624
    • Row, P.E.1
  • 75
    • 65549163770 scopus 로고    scopus 로고
    • Monoubiquitinylation regulates endosomal localization of Lst2, a negative regulator of EGF receptor signaling
    • Mosesson Y., et al. Monoubiquitinylation regulates endosomal localization of Lst2, a negative regulator of EGF receptor signaling. Dev. Cell 2009, 16:687-698.
    • (2009) Dev. Cell , vol.16 , pp. 687-698
    • Mosesson, Y.1
  • 76
    • 0035149694 scopus 로고    scopus 로고
    • Domains of Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis
    • Dunn R., Hicke L. Domains of Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis. Mol. Biol. Cell 2001, 12:421-435.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 421-435
    • Dunn, R.1    Hicke, L.2
  • 77
    • 0035854827 scopus 로고    scopus 로고
    • Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis
    • Dunn R., Hicke L. Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis. J. Biol. Chem. 2001, 276:25974-25981.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25974-25981
    • Dunn, R.1    Hicke, L.2
  • 78
    • 71849101657 scopus 로고    scopus 로고
    • The function of yeast Epsin and Ede1 ubiquitin-binding domains during receptor internalization
    • Dores M.R., et al. The function of yeast Epsin and Ede1 ubiquitin-binding domains during receptor internalization. Traffic 2010, 11:151-160.
    • (2010) Traffic , vol.11 , pp. 151-160
    • Dores, M.R.1
  • 79
    • 0038165439 scopus 로고    scopus 로고
    • Vps9p CUE domain ubiquitin binding is required for efficient endocytic protein traffic
    • Davies B.A., et al. Vps9p CUE domain ubiquitin binding is required for efficient endocytic protein traffic. J. Biol. Chem. 2003, 278:19826-19833.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19826-19833
    • Davies, B.A.1
  • 80
    • 34249947558 scopus 로고    scopus 로고
    • Ubiquitination screen using protein microarrays for comprehensive identification of Rsp5 substrates in yeast
    • Gupta R., et al. Ubiquitination screen using protein microarrays for comprehensive identification of Rsp5 substrates in yeast. Mol. Syst. Biol. 2007, 3:116.
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 116
    • Gupta, R.1
  • 81
    • 39049148016 scopus 로고    scopus 로고
    • Functional dissection of a HECT ubiquitin E3 ligase
    • Lu J.y., et al. Functional dissection of a HECT ubiquitin E3 ligase. Mol. Cell Proteomics 2008, 7:35-45.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 35-45
    • Lu, J.1
  • 82
    • 0345616428 scopus 로고    scopus 로고
    • A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
    • Shih S.C., et al. A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain. EMBO J. 2003, 22:1273-1281.
    • (2003) EMBO J. , vol.22 , pp. 1273-1281
    • Shih, S.C.1
  • 83
    • 1942437556 scopus 로고    scopus 로고
    • The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167
    • Stamenova S.D., et al. The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167. J. Biol. Chem. 2004, 279:16017-16025.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16017-16025
    • Stamenova, S.D.1
  • 84
    • 33845970909 scopus 로고    scopus 로고
    • The deubiquitinating enzyme Ubp2 modulates Rsp5-dependent Lys63-linked polyubiquitin conjugates in Saccharomyces cerevisiae
    • Kee Y., et al. The deubiquitinating enzyme Ubp2 modulates Rsp5-dependent Lys63-linked polyubiquitin conjugates in Saccharomyces cerevisiae. J. Biol. Chem. 2006, 281:36724-36731.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36724-36731
    • Kee, Y.1
  • 85
    • 33644543442 scopus 로고    scopus 로고
    • Transferrin receptor-like proteins control the degradation of a yeast metal transporter
    • Stimpson H.E.M., et al. Transferrin receptor-like proteins control the degradation of a yeast metal transporter. EMBO J. 2006, 25:662-672.
    • (2006) EMBO J. , vol.25 , pp. 662-672
    • Stimpson, H.E.M.1
  • 86
    • 1942439642 scopus 로고    scopus 로고
    • Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins
    • Hettema E.H., et al. Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins. EMBO J. 2004, 23:1279-1288.
    • (2004) EMBO J. , vol.23 , pp. 1279-1288
    • Hettema, E.H.1
  • 87
    • 33646162635 scopus 로고    scopus 로고
    • GRKs and beta-arrestins: roles in receptor silencing, trafficking and signaling
    • Reiter E., Lefkowitz R.J. GRKs and beta-arrestins: roles in receptor silencing, trafficking and signaling. Trends Endocrinol. Metab. 2006, 17:159-165.
    • (2006) Trends Endocrinol. Metab. , vol.17 , pp. 159-165
    • Reiter, E.1    Lefkowitz, R.J.2
  • 88
    • 33846137688 scopus 로고    scopus 로고
    • Hse1, a component of the Yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies
    • Ren J., et al. Hse1, a component of the Yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies. Mol. Biol. Cell 2007, 18:324-335.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 324-335
    • Ren, J.1
  • 89
    • 30944464589 scopus 로고    scopus 로고
    • Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery
    • McCullough J., et al. Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery. Curr. Biol. 2006, 16:160-165.
    • (2006) Curr. Biol. , vol.16 , pp. 160-165
    • McCullough, J.1
  • 90
    • 33750302074 scopus 로고    scopus 로고
    • Endocytosis: the DUB version
    • Clague M.J., Urbe S. Endocytosis: the DUB version. Trends Cell Biol. 2006, 16:551-559.
    • (2006) Trends Cell Biol. , vol.16 , pp. 551-559
    • Clague, M.J.1    Urbe, S.2
  • 91
    • 0033021618 scopus 로고    scopus 로고
    • Mutational analysis of Saccharomyces cerevisiae Smf1p, a member of the Nramp family of metal transporters
    • Liu X.F., Culotta V.C. Mutational analysis of Saccharomyces cerevisiae Smf1p, a member of the Nramp family of metal transporters. J. Mol. Biol. 1999, 289:885-891.
    • (1999) J. Mol. Biol. , vol.289 , pp. 885-891
    • Liu, X.F.1    Culotta, V.C.2
  • 92
    • 66349086108 scopus 로고    scopus 로고
    • Molecular mechanisms controlling phosphate-induced downregulation of the yeast Pho84 phosphate transporter
    • Lundh F., et al. Molecular mechanisms controlling phosphate-induced downregulation of the yeast Pho84 phosphate transporter. Biochemistry 2009, 48:4497-4505.
    • (2009) Biochemistry , vol.48 , pp. 4497-4505
    • Lundh, F.1
  • 93
    • 23144452091 scopus 로고    scopus 로고
    • Ubiquitin-binding domains
    • Hicke L., et al. Ubiquitin-binding domains. Nat. Rev. Mol. Cell Biol. 2005, 6:610-621.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 610-621
    • Hicke, L.1
  • 94
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu P., et al. Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 2009, 137:133-145.
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1
  • 95
    • 0036922992 scopus 로고    scopus 로고
    • Structural properties of polyubiquitin chains in solution
    • Varadan R., et al. Structural properties of polyubiquitin chains in solution. J. Mol. Biol. 2002, 324:637-647.
    • (2002) J. Mol. Biol. , vol.324 , pp. 637-647
    • Varadan, R.1
  • 96
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • Thrower J.S., et al. Recognition of the polyubiquitin proteolytic signal. EMBO J. 2000, 19:94-102.
    • (2000) EMBO J. , vol.19 , pp. 94-102
    • Thrower, J.S.1
  • 97
    • 1342304089 scopus 로고    scopus 로고
    • Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling
    • Varadan R., et al. Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling. J. Biol. Chem. 2004, 279:7055-7063.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7055-7063
    • Varadan, R.1
  • 98
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • Mukhopadhyay D., Riezman H. Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 2007, 315:201-205.
    • (2007) Science , vol.315 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 99
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains - from structures to functions
    • Dikic I., et al. Ubiquitin-binding domains - from structures to functions. Nat. Rev. Mol. Cell Biol. 2009, 10:659-671.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 659-671
    • Dikic, I.1
  • 100
    • 3042723253 scopus 로고    scopus 로고
    • Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body
    • Eugster A., et al. Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. Mol. Biol. Cell 2004, 15:3031-3041.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3031-3041
    • Eugster, A.1
  • 101
    • 34548546480 scopus 로고    scopus 로고
    • Regulation of copper-dependent endocytosis and vacuolar degradation of the yeast copper transporter, Ctr1p, by the Rsp5 ubiquitin ligase
    • Liu J., et al. Regulation of copper-dependent endocytosis and vacuolar degradation of the yeast copper transporter, Ctr1p, by the Rsp5 ubiquitin ligase. Traffic 2007, 8:1375-1384.
    • (2007) Traffic , vol.8 , pp. 1375-1384
    • Liu, J.1
  • 102
    • 0034604290 scopus 로고    scopus 로고
    • Casein kinase i-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease
    • Marchal C., et al. Casein kinase i-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease. J. Biol. Chem. 2000, 275:23608-23614.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23608-23614
    • Marchal, C.1
  • 103
    • 0032424416 scopus 로고    scopus 로고
    • Catabolite inactivation of the high-affinity hexose transporters Hxt6 and Hxt7 of Saccharomyces cerevisiae occurs in the vacuole after internalization by endocytosis
    • Krampe S., et al. Catabolite inactivation of the high-affinity hexose transporters Hxt6 and Hxt7 of Saccharomyces cerevisiae occurs in the vacuole after internalization by endocytosis. FEBS Lett. 1998, 441:343-347.
    • (1998) FEBS Lett. , vol.441 , pp. 343-347
    • Krampe, S.1


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