메뉴 건너뛰기




Volumn 59, Issue 4, 2013, Pages 207-230

Endocytic regulation of alkali metal transport proteins in mammals, yeast and plants

Author keywords

Endocytic regulation; ESCRT; Ion homeostasis; Ubiquitylation

Indexed keywords

ALKALI METAL TRANSPORT PROTEIN; ANTIPORTER; CARRIER PROTEIN; ESCRT PROTEIN; PROTEIN NHX1; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG;

EID: 84886953381     PISSN: 01728083     EISSN: 14320983     Source Type: Journal    
DOI: 10.1007/s00294-013-0401-2     Document Type: Article
Times cited : (13)

References (254)
  • 1
    • 0142123218 scopus 로고    scopus 로고
    • Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2
    • 1:CAS:528:DC%2BD3sXosFOgsbY%3D 14560004
    • Abe F, Iida H (2003) Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2. Mol Cell Biol 23:7566-7584
    • (2003) Mol Cell Biol , vol.23 , pp. 7566-7584
    • Abe, F.1    Iida, H.2
  • 4
    • 49549116213 scopus 로고    scopus 로고
    • On the origins of arrestin and rhodopsin
    • 10.1186/1471-2148-8-222 18664266
    • Alvarez CE (2008) On the origins of arrestin and rhodopsin. BMC Evol Biol 8:222. doi: 10.1186/1471-2148-8-222
    • (2008) BMC Evol Biol , vol.8 , pp. 222
    • Alvarez, C.E.1
  • 5
    • 0033786796 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways
    • 1:CAS:528:DC%2BD3cXnslWnt7w%3D 11029042
    • Amerik AY, Nowak J, Swaminathan S, Hochstrasser M (2000) The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol Biol Cell 11:3365-3380
    • (2000) Mol Biol Cell , vol.11 , pp. 3365-3380
    • Amerik, A.Y.1    Nowak, J.2    Swaminathan, S.3    Hochstrasser, M.4
  • 6
    • 0026597932 scopus 로고
    • Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cerevisiae
    • 1:CAS:528:DyaK3sXitV2ntL4%3D 1570292
    • Anderson JA, Huprikar SS, Kochian LV, Lucas WJ, Gaber RF (1992) Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 89:3736-3740
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3736-3740
    • Anderson, J.A.1    Huprikar, S.S.2    Kochian, L.V.3    Lucas, W.J.4    Gaber, R.F.5
  • 7
    • 0028702006 scopus 로고
    • + channels in Saccharomyces cerevisiae: Strategies for molecular analysis of structure and function
    • 1:STN:280:DyaK2MzitVyisA%3D%3D 7597651
    • + channels in Saccharomyces cerevisiae: strategies for molecular analysis of structure and function. Symp Soc Exp Biol 48:85-97
    • (1994) Symp Soc Exp Biol , vol.48 , pp. 85-97
    • Anderson, J.A.1    Nakamura, R.L.2    Gaber, R.F.3
  • 8
    • 0029869843 scopus 로고    scopus 로고
    • An endosomal beta COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes
    • 1:CAS:528:DyaK28XitVCht7Y%3D 8601610
    • Aniento F, Gu F, Parton RG, Gruenberg J (1996) An endosomal beta COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes. J Cell Biol 133:29-41
    • (1996) J Cell Biol , vol.133 , pp. 29-41
    • Aniento, F.1    Gu, F.2    Parton, R.G.3    Gruenberg, J.4
  • 10
    • 77749292435 scopus 로고    scopus 로고
    • Alkali metal cation transport and homeostasis in yeasts
    • 10.1128/mmbr.00042-09 1:CAS:528:DC%2BC3cXkvFOksr8%3D 20197501
    • Arino J, Ramos J, Sychrova H (2010) Alkali metal cation transport and homeostasis in yeasts. Microbiol mol biol rev 74:95-120. doi: 10.1128/mmbr.00042-09
    • (2010) Microbiol Mol Biol Rev , vol.74 , pp. 95-120
    • Arino, J.1    Ramos, J.2    Sychrova, H.3
  • 11
    • 13744263015 scopus 로고    scopus 로고
    • Novel interaction between Apc5p and Rsp5p in an intracellular signaling pathway in Saccharomyces cerevisiae
    • 10.1128/EC.4.1.134-146.2005 1:CAS:528:DC%2BD2MXhtlOht7Y%3D 15643069
    • Arnason TG, Pisclevich MG, Dash MD, Davies GF, Harkness TA (2005) Novel interaction between Apc5p and Rsp5p in an intracellular signaling pathway in Saccharomyces cerevisiae. Eukaryot Cell 4:134-146. doi: 10.1128/EC.4.1.134-146. 2005
    • (2005) Eukaryot Cell , vol.4 , pp. 134-146
    • Arnason, T.G.1    Pisclevich, M.G.2    Dash, M.D.3    Davies, G.F.4    Harkness, T.A.5
  • 13
    • 37749048772 scopus 로고    scopus 로고
    • ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1
    • 10.1016/j.devcel.2007.10.021 1:CAS:528:DC%2BD1cXhtFyjtL8%3D 18194652
    • Azmi IF, Davies BA, Xiao J, Babst M, Xu Z, Katzmann DJ (2008) ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1. Dev Cell 14:50-61. doi: 10.1016/j.devcel.2007.10.021
    • (2008) Dev Cell , vol.14 , pp. 50-61
    • Azmi, I.F.1    Davies, B.A.2    Xiao, J.3    Babst, M.4    Xu, Z.5    Katzmann, D.J.6
  • 14
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • 1:CAS:528:DC%2BD38Xmtl2it7c%3D 12194857
    • Babst M, Katzmann DJ, Estepa-Sabal EJ, Meerloo T, Emr SD (2002a) Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev Cell 3:271-282
    • (2002) Dev Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 15
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • 1:CAS:528:DC%2BD38Xmtl2itL4%3D 12194858
    • Babst M, Katzmann DJ, Snyder WB, Wendland B, Emr SD (2002b) Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev Cell 3:283-289
    • (2002) Dev Cell , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Snyder, W.B.3    Wendland, B.4    Emr, S.D.5
  • 16
    • 4344570298 scopus 로고    scopus 로고
    • The growth-regulatory protein HCRP1/hVps37A is a subunit of mammalian ESCRT-I and mediates receptor down-regulation
    • 10.1091/mbc.E04-03-0250 1:CAS:528:DC%2BD2cXnt1ekt74%3D 15240819
    • Bache KG, Slagsvold T, Cabezas A, Rosendal KR, Raiborg C, Stenmark H (2004) The growth-regulatory protein HCRP1/hVps37A is a subunit of mammalian ESCRT-I and mediates receptor down-regulation. Mol Biol Cell 15:4337-4346. doi: 10.1091/mbc.E04-03-0250
    • (2004) Mol Biol Cell , vol.15 , pp. 4337-4346
    • Bache, K.G.1    Slagsvold, T.2    Cabezas, A.3    Rosendal, K.R.4    Raiborg, C.5    Stenmark, H.6
  • 18
    • 75749102524 scopus 로고    scopus 로고
    • Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein
    • 10.1016/j.virol.2009.11.010 1:CAS:528:DC%2BC3cXhslSnu7o%3D 20004458
    • Barajas D, Nagy PD (2010) Ubiquitination of tombusvirus p33 replication protein plays a role in virus replication and binding to the host Vps23p ESCRT protein. Virology 397:358-368. doi: 10.1016/j.virol.2009.11.010
    • (2010) Virology , vol.397 , pp. 358-368
    • Barajas, D.1    Nagy, P.D.2
  • 19
    • 74549189980 scopus 로고    scopus 로고
    • A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus
    • 10.1371/journal.ppat.1000705 20041173
    • Barajas D, Jiang Y, Nagy PD (2009) A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus. PLoS Pathog 5:e1000705. doi: 10.1371/journal.ppat.1000705
    • (2009) PLoS Pathog , vol.5 , pp. 1000705
    • Barajas, D.1    Jiang, Y.2    Nagy, P.D.3
  • 20
    • 80052001379 scopus 로고    scopus 로고
    • Monoubiquitin-dependent endocytosis of the iron-regulated transporter 1 (IRT1) transporter controls iron uptake in plants
    • 10.1073/pnas.1100659108 1:CAS:528:DC%2BC3MXhtVGqt7bL 21628566
    • Barberon M, Zelazny E, Robert S, Conéjéro G, Curie C, Friml J, Vert G (2011) Monoubiquitin-dependent endocytosis of the iron-regulated transporter 1 (IRT1) transporter controls iron uptake in plants. Proc Natl Acad Sci USA 108:E450-E458. doi: 10.1073/pnas.1100659108
    • (2011) Proc Natl Acad Sci USA , vol.108
    • Barberon, M.1    Zelazny, E.2    Robert, S.3    Conéjéro, G.4    Curie, C.5    Friml, J.6    Vert, G.7
  • 21
    • 84860162235 scopus 로고    scopus 로고
    • Ion exchangers NHX1 and NHX2 mediate active potassium uptake into vacuoles to regulate cell turgor and stomatal function in Arabidopsis
    • 10.1105/tpc.111.095273 22438021
    • Barragán V, Leidi EO, Andrés Z, Rubio L, De Luca A, Fernández JA, Cubero B, Pardo JM (2012) Ion exchangers NHX1 and NHX2 mediate active potassium uptake into vacuoles to regulate cell turgor and stomatal function in Arabidopsis. Plant Cell 24:1127-1142. doi: 10.1105/tpc.111.095273
    • (2012) Plant Cell , vol.24 , pp. 1127-1142
    • Barragán, V.1    Leidi, E.O.2    Andrés, Z.3    Rubio, L.4    De Luca, A.5    Fernández, J.A.6    Cubero, B.7    Pardo, J.M.8
  • 23
    • 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
    • 1:CAS:528:DyaK1MXmtlals7s%3D 10490634
    • Beaudenon SL, Huacani MR, Wang G, McDonnell DP, Huibregtse JM (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
  • 27
    • 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
    • 10.1091/mbc.E03-04-0202 1:CAS:528:DC%2BD2cXhtlGlsro%3D 14657252
    • Blondel MO, Morvan J, Dupre S, Urban-Grimal D, Haguenauer-Tsapis R, Volland C (2004) Direct sorting of the yeast uracil permease to the endosomal system is controlled by uracil binding and Rsp5p-dependent ubiquitylation. Mol Biol Cell 15:883-895. doi: 10.1091/mbc.E03-04-0202
    • (2004) Mol Biol Cell , vol.15 , pp. 883-895
    • Blondel, M.O.1    Morvan, J.2    Dupre, S.3    Urban-Grimal, D.4    Haguenauer-Tsapis, R.5    Volland, C.6
  • 29
    • 57649231743 scopus 로고    scopus 로고
    • Modulation of the voltage-gated potassium channel Kv1.5 by the SGK1 protein kinase involves inhibition of channel ubiquitination
    • 10.1159/000185543 1:CAS:528:DC%2BD1cXhsV2lt7fF 19088441
    • Boehmer C, Laufer J, Jeyaraj S, Klaus F, Lindner R, Lang F, Palmada M (2008) Modulation of the voltage-gated potassium channel Kv1.5 by the SGK1 protein kinase involves inhibition of channel ubiquitination. Cell Physiol Biochem 22:591-600. doi: 10.1159/000185543
    • (2008) Cell Physiol Biochem , vol.22 , pp. 591-600
    • Boehmer, C.1    Laufer, J.2    Jeyaraj, S.3    Klaus, F.4    Lindner, R.5    Lang, F.6    Palmada, M.7
  • 30
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • 10.1146/annurev.biochem.72.121801.161800 1:CAS:528:DC%2BD3sXntFSgtLc%3D 12651740
    • Bonifacino JS, Traub LM (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 72:395-447. doi: 10.1146/annurev.biochem.72.121801.161800
    • (2003) Annu Rev Biochem , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 31
    • 0033638350 scopus 로고    scopus 로고
    • The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae
    • 1:CAS:528:DC%2BD3cXovFansbo%3D 11102523
    • Bowers K, Levi BP, Patel FI, Stevens TH (2000) The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae. Mol Biol Cell 11:4277-4294
    • (2000) Mol Biol Cell , vol.11 , pp. 4277-4294
    • Bowers, K.1    Levi, B.P.2    Patel, F.I.3    Stevens, T.H.4
  • 32
    • 14844311968 scopus 로고    scopus 로고
    • + exchanger Nhx1 regulates cellular pH to control vesicle trafficking
    • 10.1091/mbc.E04-11-0999 1:CAS:528:DC%2BD2MXit1SrtLw%3D 15635088
    • + exchanger Nhx1 regulates cellular pH to control vesicle trafficking. Mol Biol Cell 16:1396-1405. doi: 10.1091/mbc.E04-11-0999
    • (2005) Mol Biol Cell , vol.16 , pp. 1396-1405
    • Brett, C.L.1    Tukaye, D.N.2    Mukherjee, S.3    Rao, R.4
  • 34
    • 84869220280 scopus 로고    scopus 로고
    • SNF8, a member of the ESCRT-II complex, interacts with TRPC6 and enhances its channel activity
    • 10.1186/1471-2121-13-33 1:CAS:528:DC%2BC3sXht1yrsLg%3D 23171048
    • Carrasquillo R, Tian D, Krishna S, Pollak MR, Greka A, Schlöndorff J (2012) SNF8, a member of the ESCRT-II complex, interacts with TRPC6 and enhances its channel activity. BMC Cell Biol 13:33. doi: 10.1186/1471-2121-13-33
    • (2012) BMC Cell Biol , vol.13 , pp. 33
    • Carrasquillo, R.1    Tian, D.2    Krishna, S.3    Pollak, M.R.4    Greka, A.5    Schlöndorff, J.6
  • 35
    • 84885037043 scopus 로고    scopus 로고
    • Plant E3 Ligases: Flexible enzymes in a sessile world1
    • 10.1093/mp/sst005
    • Chen L, Hellmann H (2013) Plant E3 Ligases: flexible enzymes in a sessile world1. Mol Plant. doi: 10.1093/mp/sst005
    • (2013) Mol Plant
    • Chen, L.1    Hellmann, H.2
  • 36
    • 34547151023 scopus 로고    scopus 로고
    • A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence
    • 10.1038/nature05999 1:CAS:528:DC%2BD2sXotFajur0%3D 17625569
    • Chinchilla D, Zipfel C, Robatzek S, Kemmerling B, Nürnberger T, Jones JD, Felix G, Boller T (2007) A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence. Nature 448:497-500. doi: 10.1038/nature05999
    • (2007) Nature , vol.448 , pp. 497-500
    • Chinchilla, D.1    Zipfel, C.2    Robatzek, S.3    Kemmerling, B.4    Nürnberger, T.5    Jones, J.D.6    Felix, G.7    Boller, T.8
  • 37
    • 84861426515 scopus 로고    scopus 로고
    • Disruption of E3 ligase NEDD4 in peripheral neurons interrupts axon outgrowth: Linkage to PTEN
    • 10.1016/j.mcn.2012.04.006 1:CAS:528:DC%2BC38XptVKhsrY%3D 22561198
    • Christie KJ, Martinez JA, Zochodne DW (2012) Disruption of E3 ligase NEDD4 in peripheral neurons interrupts axon outgrowth: linkage to PTEN. Mol Cell Neurosci 50:179-192. doi: 10.1016/j.mcn.2012.04.006
    • (2012) Mol Cell Neurosci , vol.50 , pp. 179-192
    • Christie, K.J.1    Martinez, J.A.2    Zochodne, D.W.3
  • 38
    • 84866006042 scopus 로고    scopus 로고
    • Governance of endocytic trafficking and signaling by reversible ubiquitylation
    • 10.1016/j.devcel.2012.08.011 1:CAS:528:DC%2BC38Xhtlerur3J 22975321
    • Clague MJ, Liu H, Urbé S (2012) Governance of endocytic trafficking and signaling by reversible ubiquitylation. Dev Cell 23:457-467. doi: 10.1016/j.devcel.2012.08.011
    • (2012) Dev Cell , vol.23 , pp. 457-467
    • Clague, M.J.1    Liu, H.2    Urbé, S.3
  • 40
    • 78650108672 scopus 로고    scopus 로고
    • The yeast vps class e mutants: The beginning of the molecular genetic analysis of multivesicular body biogenesis
    • 10.1091/mbc.E09-07-0603 1:CAS:528:DC%2BC3MXis1OmtA%3D%3D 21115849
    • Coonrod EM, Stevens TH (2010) The yeast vps class E mutants: the beginning of the molecular genetic analysis of multivesicular body biogenesis. Mol Biol Cell 21:4057-4060. doi: 10.1091/mbc.E09-07-0603
    • (2010) Mol Biol Cell , vol.21 , pp. 4057-4060
    • Coonrod, E.M.1    Stevens, T.H.2
  • 41
    • 0035860714 scopus 로고    scopus 로고
    • The GATA transcription factors GLN3 and GAT1 link TOR to salt stress in Saccharomyces cerevisiae
    • 10.1074/jbc.M103601200 1:CAS:528:DC%2BD3MXmvFClsb4%3D 11457832
    • Crespo JL, Daicho K, Ushimaru T, Hall MN (2001) The GATA transcription factors GLN3 and GAT1 link TOR to salt stress in Saccharomyces cerevisiae. J Biol Chem 276:34441-34444. doi: 10.1074/jbc.M103601200
    • (2001) J Biol Chem , vol.276 , pp. 34441-34444
    • Crespo, J.L.1    Daicho, K.2    Ushimaru, T.3    Hall, M.N.4
  • 43
    • 0141567486 scopus 로고    scopus 로고
    • The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis: UPL3 has a specific role in trichome development
    • 1:CAS:528:DC%2BD3sXot1Oqurw%3D 12969426
    • Downes BP, Stupar RM, Gingerich DJ, Vierstra RD (2003) The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis: UPL3 has a specific role in trichome development. Plant J 35:729-742
    • (2003) Plant J , vol.35 , pp. 729-742
    • Downes, B.P.1    Stupar, R.M.2    Gingerich, D.J.3    Vierstra, R.D.4
  • 44
    • 84855665986 scopus 로고    scopus 로고
    • + channel activity with vegetative growth
    • 10.1111/j.1365-313X.2011.04786.x 1:CAS:528:DC%2BC38XhsFynsbg%3D 21914010
    • + channel activity with vegetative growth. Plant J 69:241-251. doi: 10.1111/j.1365-313X.2011.04786.x
    • (2012) Plant J , vol.69 , pp. 241-251
    • Eisenach, C.1    Chen, Z.H.2    Grefen, C.3    Blatt, M.R.4
  • 45
    • 34249688622 scopus 로고    scopus 로고
    • Regulation of the voltage-gated K(+) channels KCNQ2/3 and KCNQ3/5 by ubiquitination. Novel role for Nedd4-2
    • 10.1074/jbc.M609385200 1:CAS:528:DC%2BD2sXktFeltb0%3D 17322297
    • Ekberg J, Schuetz F, Boase NA, Conroy SJ, Manning J, Kumar S, Poronnik P, Adams DJ (2007) Regulation of the voltage-gated K(+) channels KCNQ2/3 and KCNQ3/5 by ubiquitination. Novel role for Nedd4-2. J Biol Chem 282:12135-12142. doi: 10.1074/jbc.M609385200
    • (2007) J Biol Chem , vol.282 , pp. 12135-12142
    • Ekberg, J.1    Schuetz, F.2    Boase, N.A.3    Conroy, S.J.4    Manning, J.5    Kumar, S.6    Poronnik, P.7    Adams, D.J.8
  • 47
    • 84934441798 scopus 로고    scopus 로고
    • Reconstructing the evolution of the endocytic system: Insights from genomics and molecular cell biology
    • 10.1007/978-0-387-74021-8-7 17977461
    • Field MC, Gabernet-Castello C, Dacks JB (2007) Reconstructing the evolution of the endocytic system: insights from genomics and molecular cell biology. Adv Exp Med Biol 607:84-96. doi: 10.1007/978-0-387-74021-8-7
    • (2007) Adv Exp Med Biol , vol.607 , pp. 84-96
    • Field, M.C.1    Gabernet-Castello, C.2    Dacks, J.B.3
  • 48
    • 0033553857 scopus 로고    scopus 로고
    • A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae
    • 1:CAS:528:DyaK1MXjvVKiurs%3D 10366593
    • Fisk HA, Yaffe MP (1999) A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J Cell Biol 145:1199-1208
    • (1999) J Cell Biol , vol.145 , pp. 1199-1208
    • Fisk, H.A.1    Yaffe, M.P.2
  • 49
    • 77649140362 scopus 로고    scopus 로고
    • The late endosome is essential for mTORC1 signaling
    • 10.1091/mbc.E09-09-0756 1:CAS:528:DC%2BC3cXjs1ert7s%3D 20053679
    • Flinn RJ, Yan Y, Goswami S, Parker PJ, Backer JM (2010) The late endosome is essential for mTORC1 signaling. Mol Biol Cell 21:833-841. doi: 10.1091/mbc.E09-09-0756
    • (2010) Mol Biol Cell , vol.21 , pp. 833-841
    • Flinn, R.J.1    Yan, Y.2    Goswami, S.3    Parker, P.J.4    Backer, J.M.5
  • 50
    • 3142725082 scopus 로고    scopus 로고
    • Regulation of neuronal voltage-gated sodium channels by the ubiquitin-protein ligases Nedd4 and Nedd4-2
    • 10.1074/jbc.M402820200 1:CAS:528:DC%2BD2cXlsVCntr8%3D 15123669
    • Fotia AB, Ekberg J, Adams DJ, Cook DI, Poronnik P, Kumar S (2004) Regulation of neuronal voltage-gated sodium channels by the ubiquitin-protein ligases Nedd4 and Nedd4-2. J Biol Chem 279:28930-28935. doi: 10.1074/jbc.M402820200
    • (2004) J Biol Chem , vol.279 , pp. 28930-28935
    • Fotia, A.B.1    Ekberg, J.2    Adams, D.J.3    Cook, D.I.4    Poronnik, P.5    Kumar, S.6
  • 51
    • 34447543021 scopus 로고    scopus 로고
    • Annexins and endocytosis
    • 10.1111/j.1600-0854.2007.00590.x 1:CAS:528:DC%2BD2sXovVylurg%3D 17547702
    • Futter CE, White IJ (2007) Annexins and endocytosis. Traffic 8:951-958. doi: 10.1111/j.1600-0854.2007.00590.x
    • (2007) Traffic , vol.8 , pp. 951-958
    • Futter, C.E.1    White, I.J.2
  • 52
    • 33846130922 scopus 로고    scopus 로고
    • Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast
    • 10.1128/MCB.00577-06 1:CAS:528:DC%2BD2sXmvVOmtQ%3D%3D 17101773
    • Gabriely G, Kama R, Gerst JE (2007) Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast. Mol Cell Biol 27:526-540. doi: 10.1128/MCB.00577-06
    • (2007) Mol Cell Biol , vol.27 , pp. 526-540
    • Gabriely, G.1    Kama, R.2    Gerst, J.E.3
  • 53
    • 0037591643 scopus 로고    scopus 로고
    • Functional analysis of the human orthologue of the RSP5-encoded ubiquitin protein ligase, hNedd4, in yeast
    • 10.1007/s00294-003-0371-x 1:CAS:528:DC%2BD3sXisleqtrw%3D 12684839
    • Gajewska B, Shcherbik N, Oficjalska D, Haines DS, Zoladek T (2003) Functional analysis of the human orthologue of the RSP5-encoded ubiquitin protein ligase, hNedd4, in yeast. Curr Genet 43:1-10. doi: 10.1007/s00294-003- 0371-x
    • (2003) Curr Genet , vol.43 , pp. 1-10
    • Gajewska, B.1    Shcherbik, N.2    Oficjalska, D.3    Haines, D.S.4    Zoladek, T.5
  • 54
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • 1:CAS:528:DyaK28XivVaqu7c%3D 8631913
    • Galan JM, Moreau V, Andre B, Volland C, Haguenauer-Tsapis R (1996) Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J Biol Chem 271:10946-10952
    • (1996) J Biol Chem , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    Andre, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 55
    • 84876513409 scopus 로고    scopus 로고
    • UUCD: A family-based database of ubiquitin and ubiquitin-like conjugation
    • 10.1093/nar/gks1103 1:CAS:528:DC%2BC38XhvV2ksbnJ 23172288
    • Gao T, Liu Z, Wang Y, Cheng H, Yang Q, Guo A, Ren J, Xue Y (2013) UUCD: a family-based database of ubiquitin and ubiquitin-like conjugation. Nucleic Acids Res 41:D445-D451. doi: 10.1093/nar/gks1103
    • (2013) Nucleic Acids Res , vol.41
    • Gao, T.1    Liu, Z.2    Wang, Y.3    Cheng, H.4    Yang, Q.5    Guo, A.6    Ren, J.7    Xue, Y.8
  • 56
    • 4344606680 scopus 로고    scopus 로고
    • The plant endosomal system - Its structure and role in signal transduction and plant development
    • 10.1007/s00425-004-1302-x 1:CAS:528:DC%2BD2cXmt1Gjsrk%3D 15221385
    • Geldner N (2004) The plant endosomal system - its structure and role in signal transduction and plant development. Planta 219:547-560. doi: 10.1007/s00425-004-1302-x
    • (2004) Planta , vol.219 , pp. 547-560
    • Geldner, N.1
  • 57
    • 0034161957 scopus 로고    scopus 로고
    • Zinc-regulated ubiquitin conjugation signals endocytosis of the yeast ZRT1 zinc transporter
    • 10.1042/0264-6021:3460329 1:CAS:528:DC%2BD3cXhvFSit7w%3D 10677350
    • Gitan RS, Eide DJ (2000) Zinc-regulated ubiquitin conjugation signals endocytosis of the yeast ZRT1 zinc transporter. Biochem J 346:329-336. doi: 10.1042/0264-6021:3460329
    • (2000) Biochem J , vol.346 , pp. 329-336
    • Gitan, R.S.1    Eide, D.J.2
  • 58
    • 0032582814 scopus 로고    scopus 로고
    • Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation
    • 1:CAS:528:DyaK1cXntlait7k%3D 9786854
    • Gitan RS, Luo H, Rodgers J, Broderius M, Eide D (1998) Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation. J Biol Chem 273:28617-28624
    • (1998) J Biol Chem , vol.273 , pp. 28617-28624
    • Gitan, R.S.1    Luo, H.2    Rodgers, J.3    Broderius, M.4    Eide, D.5
  • 59
    • 0033634664 scopus 로고    scopus 로고
    • FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis
    • 10911994
    • Gómez-Gómez L, Boller T (2000) FLS2: an LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis. Mol Cell 5:1003-1011
    • (2000) Mol Cell , vol.5 , pp. 1003-1011
    • Gómez-Gómez, L.1    Boller, T.2
  • 60
    • 0035979185 scopus 로고    scopus 로고
    • A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface
    • 10.1073/pnas.161282998 1:CAS:528:DC%2BD3MXlvFSkurk%3D 11481477
    • Gong X, Chang A (2001) A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface. Proc Natl Acad Sci USA 98:9104-9109. doi: 10.1073/pnas.161282998
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9104-9109
    • Gong, X.1    Chang, A.2
  • 61
    • 84866905864 scopus 로고    scopus 로고
    • Cell surface expression of human ether-a-go-go-related gene (hERG) channels is regulated by caveolin-3 protein via the ubiquitin ligase Nedd4-2
    • 10.1074/jbc.M112.389643 1:CAS:528:DC%2BC38XhsVarsLzE 22879586
    • Guo J, Wang T, Li X, Shallow H, Yang T, Li W, Xu J, Fridman MD, Yang X, Zhang S (2012) Cell surface expression of human ether-a-go-go-related gene (hERG) channels is regulated by caveolin-3 protein via the ubiquitin ligase Nedd4-2. J Biol Chem 287:33132-33141. doi: 10.1074/jbc.M112.389643
    • (2012) J Biol Chem , vol.287 , pp. 33132-33141
    • Guo, J.1    Wang, T.2    Li, X.3    Shallow, H.4    Yang, T.5    Li, W.6    Xu, J.7    Fridman, M.D.8    Yang, X.9    Zhang, S.10
  • 62
    • 17144370940 scopus 로고    scopus 로고
    • The mRNA nuclear export factor Hpr1 is regulated by Rsp5-mediated ubiquitylation
    • 10.1074/jbc.C500040200 1:CAS:528:DC%2BD2MXivV2ksbo%3D 15713680
    • Gwizdek C, Hobeika M, Kus B, Ossareh-Nazari B, Dargemont C, Rodriguez MS (2005) The mRNA nuclear export factor Hpr1 is regulated by Rsp5-mediated ubiquitylation. J Biol Chem 280:13401-13405. doi: 10.1074/jbc.C500040200
    • (2005) J Biol Chem , vol.280 , pp. 13401-13405
    • Gwizdek, C.1    Hobeika, M.2    Kus, B.3    Ossareh-Nazari, B.4    Dargemont, C.5    Rodriguez, M.S.6
  • 63
    • 34250643053 scopus 로고    scopus 로고
    • The Arabidopsis AAA ATPase SKD1 is involved in multivesicular endosome function and interacts with its positive regulator LYST-INTERACTING PROTEIN5
    • 10.1105/tpc.106.049346 1:CAS:528:DC%2BD2sXmsFeltLw%3D 17468262
    • Haas TJ, Sliwinski MK, Martínez DE, Preuss M, Ebine K, Ueda T, Nielsen E, Odorizzi G, Otegui MS (2007) The Arabidopsis AAA ATPase SKD1 is involved in multivesicular endosome function and interacts with its positive regulator LYST-INTERACTING PROTEIN5. Plant Cell 19:1295-1312. doi: 10.1105/tpc.106.049346
    • (2007) Plant Cell , vol.19 , pp. 1295-1312
    • Haas, T.J.1    Sliwinski, M.K.2    Martínez, D.E.3    Preuss, M.4    Ebine, K.5    Ueda, T.6    Nielsen, E.7    Odorizzi, G.8    Otegui, M.S.9
  • 64
    • 0036811089 scopus 로고    scopus 로고
    • The ubiquitin-dependent targeting pathway in Saccharomyces cerevisiae plays a critical role in multiple chromatin assembly regulatory steps
    • 1:CAS:528:DC%2BD38XptVOrsLs%3D 12399376
    • Harkness TA, Davies GF, Ramaswamy V, Arnason TG (2002) The ubiquitin-dependent targeting pathway in Saccharomyces cerevisiae plays a critical role in multiple chromatin assembly regulatory steps. Genetics 162:615-632
    • (2002) Genetics , vol.162 , pp. 615-632
    • Harkness, T.A.1    Davies, G.F.2    Ramaswamy, V.3    Arnason, T.G.4
  • 65
    • 14844321857 scopus 로고    scopus 로고
    • Analysis of the mKir2.1 channel activity in potassium influx defective Saccharomyces cerevisiae strains determined as changes in growth characteristics
    • 10.1016/j.febslet.2005.02.025 1:CAS:528:DC%2BD2MXitFChs7Y%3D 15757667
    • Hasenbrink G, Schwarzer S, Kolacna L, Ludwig J, Sychrova H, Lichtenberg-Fraté H (2005) Analysis of the mKir2.1 channel activity in potassium influx defective Saccharomyces cerevisiae strains determined as changes in growth characteristics. FEBS Lett 579:1723-1731. doi: 10.1016/j.febslet.2005.02.025
    • (2005) FEBS Lett , vol.579 , pp. 1723-1731
    • Hasenbrink, G.1    Schwarzer, S.2    Kolacna, L.3    Ludwig, J.4    Sychrova, H.5    Lichtenberg-Fraté, H.6
  • 66
    • 80052416211 scopus 로고    scopus 로고
    • Endocytosis of the aspartic acid/glutamic acid transporter Dip5 is triggered by substrate-dependent recruitment of the Rsp5 ubiquitin ligase via the arrestin-like protein Aly2
    • 10.1128/MCB.00464-10 1:CAS:528:DC%2BC3MXpslWitg%3D%3D 20956561
    • Hatakeyama R, Kamiya M, Takahara T, Maeda T (2010) Endocytosis of the aspartic acid/glutamic acid transporter Dip5 is triggered by substrate-dependent recruitment of the Rsp5 ubiquitin ligase via the arrestin-like protein Aly2. Mol Cell Biol 30:5598-5607. doi: 10.1128/MCB.00464-10
    • (2010) Mol Cell Biol , vol.30 , pp. 5598-5607
    • Hatakeyama, R.1    Kamiya, M.2    Takahara, T.3    Maeda, T.4
  • 67
    • 27144493736 scopus 로고    scopus 로고
    • Constitutive activation of the pH-responsive Rim101 pathway in yeast mutants defective in late steps of the MVB/ESCRT pathway
    • 10.1128/mcb.25.21.9478-9490.2005 1:CAS:528:DC%2BD2MXhtFOnsrfI 16227598
    • Hayashi M, Fukuzawa T, Sorimachi H, Maeda T (2005) Constitutive activation of the pH-responsive Rim101 pathway in yeast mutants defective in late steps of the MVB/ESCRT pathway. Mol Cell Biol 25:9478-9490. doi: 10.1128/mcb.25.21.9478-9490.2005
    • (2005) Mol Cell Biol , vol.25 , pp. 9478-9490
    • Hayashi, M.1    Fukuzawa, T.2    Sorimachi, H.3    Maeda, T.4
  • 70
    • 0028971506 scopus 로고
    • NPl1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • 1:CAS:528:DyaK2MXptlersLY%3D 8596462
    • Hein C, Springael JY, Volland C, Haguenauer-Tsapis R, André B (1995) NPl1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol Microbiol 18:77-87
    • (1995) Mol Microbiol , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    André, B.5
  • 71
    • 1842525944 scopus 로고    scopus 로고
    • + channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1
    • 10.1002/jcp.10430 1:CAS:528:DC%2BD2cXjtVamurk%3D 15040001
    • + channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1. J Cell Physiol 199:194-199. doi: 10.1002/jcp.10430
    • (2004) J Cell Physiol , vol.199 , pp. 194-199
    • Henke, G.1    Maier, G.2    Wallisch, S.3    Boehmer, C.4    Lang, F.5
  • 72
    • 84862835204 scopus 로고    scopus 로고
    • Artificial ubiquitylation is sufficient for sorting of a plasma membrane ATPase to the vacuolar lumen of Arabidopsis cells
    • 10.1007/s00425-012-1587-0 1:CAS:528:DC%2BC38XptFChu7s%3D 22258747
    • Herberth S, Shahriari M, Bruderek M, Hessner F, Müller B, Hülskamp M, Schellmann S (2012) Artificial ubiquitylation is sufficient for sorting of a plasma membrane ATPase to the vacuolar lumen of Arabidopsis cells. Planta 236:63-77. doi: 10.1007/s00425-012-1587-0
    • (2012) Planta , vol.236 , pp. 63-77
    • Herberth, S.1    Shahriari, M.2    Bruderek, M.3    Hessner, F.4    Müller, B.5    Hülskamp, M.6    Schellmann, S.7
  • 73
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • 10.1146/annurev.cellbio.19.110701.154617 1:CAS:528:DC%2BD3sXpsFamtrk%3D 14570567
    • Hicke L, Dunn R (2003) Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19:141-172. doi: 10.1146/annurev.cellbio.19.110701.154617
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 74
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • 1:CAS:528:DyaK28Xnt1egtg%3D%3D 8565073
    • Hicke L, Riezman H (1996) Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84:277-287
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 75
    • 0032550179 scopus 로고    scopus 로고
    • Cytoplasmic tail phosphorylation of the alpha-factor receptor is required for its ubiquitination and internalization
    • 1:CAS:528:DyaK1cXis1GltLY%3D 9548714
    • Hicke L, Zanolari B, Riezman H (1998) Cytoplasmic tail phosphorylation of the alpha-factor receptor is required for its ubiquitination and internalization. J Cell Biol 141:349-358
    • (1998) J Cell Biol , vol.141 , pp. 349-358
    • Hicke, L.1    Zanolari, B.2    Riezman, H.3
  • 76
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • 1:CAS:528:DC%2BD3cXmsFWit7Y%3D 11007476
    • Hoppe T, Matuschewski K, Rape M, Schlenker S, Ulrich HD, Jentsch S (2000) Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102:577-586
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 78
    • 84871868771 scopus 로고    scopus 로고
    • Cryptococcus neoformans requires the ESCRT protein Vps23 for iron acquisition from heme, for capsule formation, and for virulence
    • 10.1128/IAI.01037-12 1:CAS:528:DC%2BC3sXlt1Snu7c%3D 23132495
    • Hu G, Caza M, Cadieux B, Chan V, Liu V, Kronstad J (2013) Cryptococcus neoformans requires the ESCRT protein Vps23 for iron acquisition from heme, for capsule formation, and for virulence. Infect Immun 81:292-302. doi: 10.1128/IAI.01037-12
    • (2013) Infect Immun , vol.81 , pp. 292-302
    • Hu, G.1    Caza, M.2    Cadieux, B.3    Chan, V.4    Liu, V.5    Kronstad, J.6
  • 79
    • 33644852909 scopus 로고    scopus 로고
    • Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain
    • 10.1016/j.molcel.2006.02.018 1:CAS:528:DC%2BD28XjtVyjurc%3D 16543144
    • Huang F, Kirkpatrick D, Jiang X, Gygi S, Sorkin A (2006) Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol Cell 21:737-748. doi: 10.1016/j.molcel.2006.02.018
    • (2006) Mol Cell , vol.21 , pp. 737-748
    • Huang, F.1    Kirkpatrick, D.2    Jiang, X.3    Gygi, S.4    Sorkin, A.5
  • 80
    • 36749036679 scopus 로고    scopus 로고
    • EGF receptor ubiquitination is not necessary for its internalization
    • 10.1073/pnas.0707416104 1:CAS:528:DC%2BD2sXht1KgtLjF 17940017
    • Huang F, Goh LK, Sorkin A (2007) EGF receptor ubiquitination is not necessary for its internalization. Proc Natl Acad Sci USA 104:16904-16909. doi: 10.1073/pnas.0707416104
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16904-16909
    • Huang, F.1    Goh, L.K.2    Sorkin, A.3
  • 81
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • 1:CAS:528:DyaK2MXksl2ku7k%3D 7708685
    • Huibregtse JM, Scheffner M, Beaudenon S, Howley PM (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc Natl Acad Sci USA 92:2563-2567
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 82
    • 1042301861 scopus 로고    scopus 로고
    • Trafficking of the plant potassium inward rectifier KAT1 in guard cell protoplasts of Vicia faba
    • 1:CAS:528:DC%2BD2cXhvFejtrw%3D 14731259
    • Hurst AC, Meckel T, Tayefeh S, Thiel G, Homann U (2004) Trafficking of the plant potassium inward rectifier KAT1 in guard cell protoplasts of Vicia faba. Plant J 37:391-397
    • (2004) Plant J , vol.37 , pp. 391-397
    • Hurst, A.C.1    Meckel, T.2    Tayefeh, S.3    Thiel, G.4    Homann, U.5
  • 83
    • 84861783400 scopus 로고    scopus 로고
    • Ubiquitin-binding proteins: Decoders of ubiquitin-mediated cellular functions
    • 10.1146/annurev-biochem-051810-094654 1:CAS:528:DC%2BC38XhtVGls7bE 22482907
    • Husnjak K, Dikic I (2012) Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions. Annu Rev Biochem 81:291-322. doi: 10.1146/annurev-biochem-051810-094654
    • (2012) Annu Rev Biochem , vol.81 , pp. 291-322
    • Husnjak, K.1    Dikic, I.2
  • 84
    • 84855544418 scopus 로고    scopus 로고
    • Interactome of the plant-specific ESCRT-III component AtVPS2.2 in Arabidopsis thaliana
    • 10.1021/pr200845n 1:CAS:528:DC%2BC3MXhtlaqsb7E 22010978
    • Ibl V, Csaszar E, Schlager N, Neubert S, Spitzer C, Hauser MT (2012) Interactome of the plant-specific ESCRT-III component AtVPS2.2 in Arabidopsis thaliana. J Proteome Res 11:397-411. doi: 10.1021/pr200845n
    • (2012) J Proteome Res , vol.11 , pp. 397-411
    • Ibl, V.1    Csaszar, E.2    Schlager, N.3    Neubert, S.4    Spitzer, C.5    Hauser, M.T.6
  • 85
    • 20144386846 scopus 로고    scopus 로고
    • 14-3-3 proteins modulate the expression of epithelial Na + channels by phosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase
    • 10.1074/jbc.M412884200 1:CAS:528:DC%2BD2MXislygt7g%3D 15677482
    • Ichimura T, Yamamura H, Sasamoto K, Tominaga Y, Taoka M, Kakiuchi K, Shinkawa T, Takahashi N, Shimada S, Isobe T (2005) 14-3-3 proteins modulate the expression of epithelial Na + channels by phosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase. J Biol Chem 280:13187-13194. doi: 10.1074/jbc.M412884200
    • (2005) J Biol Chem , vol.280 , pp. 13187-13194
    • Ichimura, T.1    Yamamura, H.2    Sasamoto, K.3    Tominaga, Y.4    Taoka, M.5    Kakiuchi, K.6    Shinkawa, T.7    Takahashi, N.8    Shimada, S.9    Isobe, T.10
  • 87
    • 0030808571 scopus 로고    scopus 로고
    • Elimination of defective alpha-factor pheromone receptors
    • 1:CAS:528:DyaK2sXntVSjsLo%3D 9343384
    • Jenness DD, Li Y, Tipper C, Spatrick P (1997) Elimination of defective alpha-factor pheromone receptors. Mol Cell Biol 17:6236-6245
    • (1997) Mol Cell Biol , vol.17 , pp. 6236-6245
    • Jenness, D.D.1    Li, Y.2    Tipper, C.3    Spatrick, P.4
  • 88
    • 33847639227 scopus 로고    scopus 로고
    • The KCNQ1 potassium channel is down-regulated by ubiquitylating enzymes of the Nedd4/Nedd4-like family
    • 10.1016/j.cardiores.2007.01.008 1:CAS:528:DC%2BD2sXislWrtLo%3D 17289006
    • Jespersen T, Membrez M, Nicolas CS, Pitard B, Staub O, Olesen SP, Baró I, Abriel H (2007) The KCNQ1 potassium channel is down-regulated by ubiquitylating enzymes of the Nedd4/Nedd4-like family. Cardiovasc Res 74:64-74. doi: 10.1016/j.cardiores.2007.01.008
    • (2007) Cardiovasc Res , vol.74 , pp. 64-74
    • Jespersen, T.1    Membrez, M.2    Nicolas, C.S.3    Pitard, B.4    Staub, O.5    Olesen, S.P.6    Baró, I.7    Abriel, H.8
  • 89
    • 0034331549 scopus 로고    scopus 로고
    • Identification of multiple proteins expressed in murine embryos as binding partners for the WW domains of the ubiquitin-protein ligase Nedd4
    • 1:CAS:528:DC%2BD3cXotF2rtbk%3D 11042109
    • Jolliffe CN, Harvey KF, Haines BP, Parasivam G, Kumar S (2000) Identification of multiple proteins expressed in murine embryos as binding partners for the WW domains of the ubiquitin-protein ligase Nedd4. Biochem J 351(Pt 3):557-565
    • (2000) Biochem J , vol.351 , Issue.PART 3 , pp. 557-565
    • Jolliffe, C.N.1    Harvey, K.F.2    Haines, B.P.3    Parasivam, G.4    Kumar, S.5
  • 90
    • 83755162497 scopus 로고    scopus 로고
    • + exchanger Nhx1/Vps44 functions independently and downstream of multivesicular body formation
    • 10.1074/jbc.M111.282319 1:CAS:528:DC%2BC3MXhs1ahtbnN 21998311
    • + exchanger Nhx1/Vps44 functions independently and downstream of multivesicular body formation. J Biol Chem 286:44067-44077. doi: 10.1074/jbc.M111.282319
    • (2011) J Biol Chem , vol.286 , pp. 44067-44077
    • Kallay, L.M.1    Brett, C.L.2    Tukaye, D.N.3    Wemmer, M.A.4    Chyou, A.5    Odorizzi, G.6    Rao, R.7
  • 91
    • 38649110187 scopus 로고    scopus 로고
    • Missorting of the Aquaporin-2 mutant E258K to multivesicular bodies/lysosomes in dominant NDI is associated with its monoubiquitination and increased phosphorylation by PKC but is due to the loss of E258
    • 10.1007/s00424-007-0364-6 1:CAS:528:DC%2BD1cXhtFWktLY%3D 17965877
    • Kamsteeg EJ, Savelkoul PJ, Hendriks G, Konings IB, Nivillac NM, Lagendijk AK, van der Sluijs P, Deen PM (2008) Missorting of the Aquaporin-2 mutant E258K to multivesicular bodies/lysosomes in dominant NDI is associated with its monoubiquitination and increased phosphorylation by PKC but is due to the loss of E258. Pflugers Arch 455:1041-1054. doi: 10.1007/s00424-007-0364-6
    • (2008) Pflugers Arch , vol.455 , pp. 1041-1054
    • Kamsteeg, E.J.1    Savelkoul, P.J.2    Hendriks, G.3    Konings, I.B.4    Nivillac, N.M.5    Lagendijk, A.K.6    Van Der Sluijs, P.7    Deen, P.M.8
  • 93
    • 79953202184 scopus 로고    scopus 로고
    • High boron-induced ubiquitination regulates vacuolar sorting of the BOR1 borate transporter in Arabidopsis thaliana
    • 10.1074/jbc.M110.184929 1:CAS:528:DC%2BC3MXitVyktbg%3D 21148314
    • Kasai K, Takano J, Miwa K, Toyoda A, Fujiwara T (2011) High boron-induced ubiquitination regulates vacuolar sorting of the BOR1 borate transporter in Arabidopsis thaliana. J Biol Chem 286:6175-6183. doi: 10.1074/jbc.M110.184929
    • (2011) J Biol Chem , vol.286 , pp. 6175-6183
    • Kasai, K.1    Takano, J.2    Miwa, K.3    Toyoda, A.4    Fujiwara, T.5
  • 94
    • 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
    • 1:CAS:528:DC%2BD3MXlvVClsL8%3D 11511343
    • Katzmann DJ, Babst M, Emr SD (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
  • 95
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • 10.1083/jcb.200302136 1:CAS:528:DC%2BD3sXmt1CrurY%3D 12900393
    • Katzmann DJ, Stefan CJ, Babst M, Emr SD (2003) Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J Cell Biol 162:413-423. doi: 10.1083/jcb.200302136
    • (2003) J Cell Biol , vol.162 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 96
    • 0038136885 scopus 로고    scopus 로고
    • CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility
    • 10.1126/science.1081068 1:CAS:528:DC%2BD3sXktFGkt7s%3D 12764198
    • Kim JM, Wu H, Green G, Winkler CA, Kopp JB, Miner JH, Unanue ER, Shaw AS (2003) CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility. Science 300:1298-1300. doi: 10.1126/science.1081068
    • (2003) Science , vol.300 , pp. 1298-1300
    • Kim, J.M.1    Wu, H.2    Green, G.3    Winkler, C.A.4    Kopp, J.B.5    Miner, J.H.6    Unanue, E.R.7    Shaw, A.S.8
  • 98
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • 8045256
    • Kölling R, Hollenberg CP (1994) The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J 13:3261-3271
    • (1994) EMBO J , vol.13 , pp. 3261-3271
    • Kölling, R.1    Hollenberg, C.P.2
  • 99
    • 84861877407 scopus 로고    scopus 로고
    • The ubiquitin code
    • 10.1146/annurev-biochem-060310-170328 1:CAS:528:DC%2BC38XhtVGls7bJ 22524316
    • Komander D, Rape M (2012) The ubiquitin code. Annu Rev Biochem 81:203-229. doi: 10.1146/annurev-biochem-060310-170328
    • (2012) Annu Rev Biochem , vol.81 , pp. 203-229
    • Komander, D.1    Rape, M.2
  • 100
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation - The unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • 10.1038/nrm3394 1:CAS:528:DC%2BC38XhtVKnurnM 22820888
    • Kulathu Y, Komander D (2012) Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat Rev Mol Cell Biol 13:508-523. doi: 10.1038/nrm3394
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 101
    • 77954520146 scopus 로고    scopus 로고
    • Neurological channelopathies
    • 10.1146/annurev-neuro-060909-153122 1:CAS:528:DC%2BC3cXhsFartr3N 20331364
    • Kullmann DM (2010) Neurological channelopathies. Annu Rev Neurosci 33:151-172. doi: 10.1146/annurev-neuro-060909-153122
    • (2010) Annu Rev Neurosci , vol.33 , pp. 151-172
    • Kullmann, D.M.1
  • 102
    • 0026763128 scopus 로고
    • Identification of a set of genes with developmentally down-regulated expression in the mouse brain
    • 1:CAS:528:DyaK38Xks1Citrg%3D 1378265
    • Kumar S, Tomooka Y, Noda M (1992) Identification of a set of genes with developmentally down-regulated expression in the mouse brain. Biochem Biophys Res Commun 185:1155-1161
    • (1992) Biochem Biophys Res Commun , vol.185 , pp. 1155-1161
    • Kumar, S.1    Tomooka, Y.2    Noda, M.3
  • 103
    • 0031569413 scopus 로고    scopus 로고
    • CDNA cloning, expression analysis, and mapping of the mouse Nedd4 gene
    • 10.1006/geno.1996.4582 1:CAS:528:DyaK2sXhvF2itr8%3D 9073511
    • Kumar S, Harvey KF, Kinoshita M, Copeland NG, Noda M, Jenkins NA (1997) cDNA cloning, expression analysis, and mapping of the mouse Nedd4 gene. Genomics 40:435-443. doi: 10.1006/geno.1996.4582
    • (1997) Genomics , vol.40 , pp. 435-443
    • Kumar, S.1    Harvey, K.F.2    Kinoshita, M.3    Copeland, N.G.4    Noda, M.5    Jenkins, N.A.6
  • 104
    • 84875519176 scopus 로고    scopus 로고
    • ESCRT-III assembly and cytokinetic abscission are induced by tension release in the intercellular bridge
    • 10.1126/science.1233866 1:CAS:528:DC%2BC3sXksFOhsb4%3D 23539606
    • Lafaurie-Janvore J, Maiuri P, Wang I, Pinot M, Manneville JB, Betz T, Balland M, Piel M (2013) ESCRT-III assembly and cytokinetic abscission are induced by tension release in the intercellular bridge. Science 339:1625-1629. doi: 10.1126/science.1233866
    • (2013) Science , vol.339 , pp. 1625-1629
    • Lafaurie-Janvore, J.1    Maiuri, P.2    Wang, I.3    Pinot, M.4    Manneville, J.B.5    Betz, T.6    Balland, M.7    Piel, M.8
  • 105
    • 34249787044 scopus 로고    scopus 로고
    • Rice SCAMP1 defines clathrin-coated, trans-golgi-located tubular-vesicular structures as an early endosome in tobacco BY-2 cells
    • 10.1105/tpc.106.045708 1:CAS:528:DC%2BD2sXjtFyntLo%3D 17209124
    • Lam SK, Siu CL, Hillmer S, Jang S, An G, Robinson DG, Jiang L (2007) Rice SCAMP1 defines clathrin-coated, trans-golgi-located tubular-vesicular structures as an early endosome in tobacco BY-2 cells. Plant Cell 19:296-319. doi: 10.1105/tpc.106.045708
    • (2007) Plant Cell , vol.19 , pp. 296-319
    • Lam, S.K.1    Siu, C.L.2    Hillmer, S.3    Jang, S.4    An, G.5    Robinson, D.G.6    Jiang, L.7
  • 106
    • 84878214977 scopus 로고    scopus 로고
    • The Serum- and Glucocorticoid-Inducible Kinase SGK1 and SGK3 Regulate hERG Channel Expression via Ubiquitin Ligase Nedd4-2 and GTPase Rab11
    • 10.1074/jbc.M113.453670 23589291
    • Lamothe S, Zhang S (2013) The Serum- and Glucocorticoid-Inducible Kinase SGK1 and SGK3 Regulate hERG Channel Expression via Ubiquitin Ligase Nedd4-2 and GTPase Rab11. J Biol Chem. doi: 10.1074/jbc.M113.453670
    • (2013) J Biol Chem
    • Lamothe, S.1    Zhang, S.2
  • 108
    • 77950857969 scopus 로고    scopus 로고
    • The ubiquitin code of yeast permease trafficking
    • 10.1016/j.tcb.2010.01.004 1:CAS:528:DC%2BC3cXktlCksrY%3D 20138522
    • Lauwers E, Erpapazoglou Z, Haguenauer-Tsapis R, André B (2010) The ubiquitin code of yeast permease trafficking. Trends Cell Biol 20:196-204. doi: 10.1016/j.tcb.2010.01.004
    • (2010) Trends Cell Biol , vol.20 , pp. 196-204
    • Lauwers, E.1    Erpapazoglou, Z.2    Haguenauer-Tsapis, R.3    André, B.4
  • 109
    • 77958070740 scopus 로고    scopus 로고
    • The sodium/proton exchanger NHE8 regulates late endosomal morphology and function
    • 10.1091/mbc.E09-12-1053 1:CAS:528:DC%2BC3cXhtlGlt7%2FI 20719963
    • Lawrence SP, Bright NA, Luzio JP, Bowers K (2010) The sodium/proton exchanger NHE8 regulates late endosomal morphology and function. Mol Biol Cell 21:3540-3551. doi: 10.1091/mbc.E09-12-1053
    • (2010) Mol Biol Cell , vol.21 , pp. 3540-3551
    • Lawrence, S.P.1    Bright, N.A.2    Luzio, J.P.3    Bowers, K.4
  • 110
    • 0034680750 scopus 로고    scopus 로고
    • Acidic amino acids flanking phosphorylation sites in the M2 muscarinic receptor regulate receptor phosphorylation, internalization, and interaction with arrestins
    • 10.1074/jbc.M002225200 1:CAS:528:DC%2BD3cXosVSktrw%3D 10952973
    • Lee KB, Ptasienski JA, Bunemann M, Hosey MM (2000) Acidic amino acids flanking phosphorylation sites in the M2 muscarinic receptor regulate receptor phosphorylation, internalization, and interaction with arrestins. J Biol Chem 275:35767-35777. doi: 10.1074/jbc.M002225200
    • (2000) J Biol Chem , vol.275 , pp. 35767-35777
    • Lee, K.B.1    Ptasienski, J.A.2    Bunemann, M.3    Hosey, M.M.4
  • 111
    • 84871997901 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the ESCRT machinery in endosomal trafficking
    • 10.1083/jcb.201204137 1:CAS:528:DC%2BC38XhslOit73K 23166352
    • Lee SM, Chin LS, Li L (2012) Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the ESCRT machinery in endosomal trafficking. J Cell Biol 199:799-816. doi: 10.1083/jcb.201204137
    • (2012) J Cell Biol , vol.199 , pp. 799-816
    • Lee, S.M.1    Chin, L.S.2    Li, L.3
  • 112
    • 33751533776 scopus 로고    scopus 로고
    • New roles for beta-arrestins in cell signaling: Not just for seven-transmembrane receptors
    • 10.1016/j.molcel.2006.11.007 1:CAS:528:DC%2BD28XhtlCns7%2FL 17157248
    • Lefkowitz RJ, Rajagopal K, Whalen EJ (2006) New roles for beta-arrestins in cell signaling: not just for seven-transmembrane receptors. Mol Cell 24:643-652. doi: 10.1016/j.molcel.2006.11.007
    • (2006) Mol Cell , vol.24 , pp. 643-652
    • Lefkowitz, R.J.1    Rajagopal, K.2    Whalen, E.J.3
  • 113
    • 55549102963 scopus 로고    scopus 로고
    • Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface
    • 10.1016/j.cell.2008.09.025 1:CAS:528:DC%2BD1cXhsVCls7vI 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: 10.1016/j.cell.2008.09.025
    • (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
  • 114
    • 32244448470 scopus 로고    scopus 로고
    • Quality control of a mutant plasma membrane ATPase: Ubiquitylation prevents cell-surface stability
    • 10.1242/jcs.02749 1:CAS:528:DC%2BD28Xhs1eitb0%3D 16410553
    • Liu Y, Chang A (2006) Quality control of a mutant plasma membrane ATPase: ubiquitylation prevents cell-surface stability. J Cell Sci 119:360-369. doi: 10.1242/jcs.02749
    • (2006) J Cell Sci , vol.119 , pp. 360-369
    • Liu, Y.1    Chang, A.2
  • 115
    • 34548546480 scopus 로고    scopus 로고
    • Regulation of copper-dependent endocytosis and vacuolar degradation of the yeast copper transporter, Ctr1p, by the Rsp5 ubiquitin ligase
    • 10.1111/j.1600-0854.2007.00616.x 1:CAS:528:DC%2BD2sXhtFKms7rE 17645432
    • Liu J, Sitaram A, Burd CG (2007) Regulation of copper-dependent endocytosis and vacuolar degradation of the yeast copper transporter, Ctr1p, by the Rsp5 ubiquitin ligase. Traffic 8:1375-1384. doi: 10.1111/j.1600-0854.2007. 00616.x
    • (2007) Traffic , vol.8 , pp. 1375-1384
    • Liu, J.1    Sitaram, A.2    Burd, C.G.3
  • 116
    • 67349270258 scopus 로고    scopus 로고
    • Abnormal development of the neuromuscular junction in Nedd4-deficient mice
    • 10.1016/j.ydbio.2009.03.023 1:CAS:528:DC%2BD1MXmtVaqtrY%3D 19345204
    • Liu Y, Oppenheim RW, Sugiura Y, Lin W (2009) Abnormal development of the neuromuscular junction in Nedd4-deficient mice. Dev Biol 330:153-166. doi: 10.1016/j.ydbio.2009.03.023
    • (2009) Dev Biol , vol.330 , pp. 153-166
    • Liu, Y.1    Oppenheim, R.W.2    Sugiura, Y.3    Lin, W.4
  • 117
    • 84872412303 scopus 로고    scopus 로고
    • Posttranslational modification and trafficking of PIN auxin efflux carriers
    • 10.1016/j.mod.2012.02.003 22425600
    • Löfke C, Luschnig C, Kleine-Vehn J (2013) Posttranslational modification and trafficking of PIN auxin efflux carriers. Mech Dev 130:82-94. doi: 10.1016/j.mod.2012.02.003
    • (2013) Mech Dev , vol.130 , pp. 82-94
    • Löfke, C.1    Luschnig, C.2    Kleine-Vehn, J.3
  • 118
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- or phosphothreonine-binding modules
    • 1:CAS:528:DyaK1MXhs1Cjsbw%3D 10037602
    • Lu PJ, Zhou XZ, Shen M, Lu KP (1999) Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 283:1325-1328
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 119
    • 76249083550 scopus 로고    scopus 로고
    • A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity
    • 10.1073/pnas.0909705107 1:CAS:528:DC%2BC3cXnsVKlsQ%3D%3D 20018686
    • Lu D, Wu S, Gao X, Zhang Y, Shan L, He P (2010) A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity. Proc Natl Acad Sci USA 107:496-501. doi: 10.1073/pnas.0909705107
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 496-501
    • Lu, D.1    Wu, S.2    Gao, X.3    Zhang, Y.4    Shan, L.5    He, P.6
  • 120
    • 79959364526 scopus 로고    scopus 로고
    • Direct ubiquitination of pattern recognition receptor FLS2 attenuates plant innate immunity
    • 10.1126/science.1204903 1:CAS:528:DC%2BC3MXntlOltLs%3D 21680842
    • Lu D, Lin W, Gao X, Wu S, Cheng C, Avila J, Heese A, Devarenne TP, He P, Shan L (2011) Direct ubiquitination of pattern recognition receptor FLS2 attenuates plant innate immunity. Science 332:1439-1442. doi: 10.1126/science.1204903
    • (2011) Science , vol.332 , pp. 1439-1442
    • Lu, D.1    Lin, W.2    Gao, X.3    Wu, S.4    Cheng, C.5    Avila, J.6    Heese, A.7    Devarenne, T.P.8    He, P.9    Shan, L.10
  • 121
    • 4444342179 scopus 로고    scopus 로고
    • Bro1 coordinates deubiquitination in the multivesicular body pathway by recruiting Doa4 to endosomes
    • 10.1083/jcb.200403139 1:CAS:528:DC%2BD2cXnsVeisbs%3D 15326198
    • Luhtala N, Odorizzi G (2004) Bro1 coordinates deubiquitination in the multivesicular body pathway by recruiting Doa4 to endosomes. J Cell Biol 166:717-729. doi: 10.1083/jcb.200403139
    • (2004) J Cell Biol , vol.166 , pp. 717-729
    • Luhtala, N.1    Odorizzi, G.2
  • 122
    • 81855183664 scopus 로고    scopus 로고
    • TORC1 regulates endocytosis via Npr1-mediated phosphoinhibition of a ubiquitin ligase adaptor
    • 10.1016/j.cell.2011.09.054 1:CAS:528:DC%2BC3MXhsFeisrjK 22118465
    • MacGurn JA, Hsu PC, Smolka MB, Emr SD (2011) TORC1 regulates endocytosis via Npr1-mediated phosphoinhibition of a ubiquitin ligase adaptor. Cell 147:1104-1117. doi: 10.1016/j.cell.2011.09.054
    • (2011) Cell , vol.147 , pp. 1104-1117
    • Macgurn, J.A.1    Hsu, P.C.2    Smolka, M.B.3    Emr, S.D.4
  • 123
    • 84861867814 scopus 로고    scopus 로고
    • Ubiquitin and Membrane Protein Turnover: From Cradle to Grave
    • 10.1146/annurev-biochem-060210-093619 1:CAS:528:DC%2BC38XhtVGls7bK 22404628
    • MacGurn JA, Hsu P-C, Emr SD (2012) Ubiquitin and Membrane Protein Turnover: from Cradle to Grave. Annu Rev Biochem 81(81):231-259. doi: 10.1146/annurev-biochem-060210-093619
    • (2012) Annu Rev Biochem , vol.81 , Issue.81 , pp. 231-259
    • Macgurn, J.A.1    Hsu, P.-C.2    Emr, S.D.3
  • 125
    • 0037926403 scopus 로고    scopus 로고
    • Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells
    • 10.1093/emboj/cdg321 1:CAS:528:DC%2BD3sXltFyht7c%3D 12839987
    • Mayran N, Parton RG, Gruenberg J (2003) Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells. EMBO J 22:3242-3253. doi: 10.1093/emboj/cdg321
    • (2003) EMBO J , vol.22 , pp. 3242-3253
    • Mayran, N.1    Parton, R.G.2    Gruenberg, J.3
  • 126
    • 3242713378 scopus 로고    scopus 로고
    • Endocytosis against high turgor: Intact guard cells of Vicia faba constitutively endocytose fluorescently labelled plasma membrane and GFP-tagged K-channel KAT1
    • 10.1111/j.1365-313X.2004.02119.x 1:CAS:528:DC%2BD2cXntFGrt78%3D 15225284
    • Meckel T, Hurst AC, Thiel G, Homann U (2004) Endocytosis against high turgor: intact guard cells of Vicia faba constitutively endocytose fluorescently labelled plasma membrane and GFP-tagged K-channel KAT1. Plant J 39:182-193. doi: 10.1111/j.1365-313X.2004.02119.x
    • (2004) Plant J , vol.39 , pp. 182-193
    • Meckel, T.1    Hurst, A.C.2    Thiel, G.3    Homann, U.4
  • 127
    • 84868676870 scopus 로고    scopus 로고
    • Internal amino acids promote Gap1 permease ubiquitylation via TORC1/Npr1/14-3-3-dependent control of the Bul arrestin-like adaptors
    • 10.1128/MCB.00463-12 1:CAS:528:DC%2BC38Xhs1Cjur3I 22966204
    • Merhi A, André B (2012) Internal amino acids promote Gap1 permease ubiquitylation via TORC1/Npr1/14-3-3-dependent control of the Bul arrestin-like adaptors. Mol Cell Biol 32:4510-4522. doi: 10.1128/MCB.00463-12
    • (2012) Mol Cell Biol , vol.32 , pp. 4510-4522
    • Merhi, A.1    André, B.2
  • 128
    • 84858142724 scopus 로고    scopus 로고
    • HECT and RING finger families of E3 ubiquitin ligases at a glance
    • 10.1242/jcs.091777 1:CAS:528:DC%2BC38Xlt1Oltbc%3D 22389392
    • Metzger MB, Hristova VA, Weissman AM (2012) HECT and RING finger families of E3 ubiquitin ligases at a glance. J Cell Sci 125:531-537. doi: 10.1242/jcs.091777
    • (2012) J Cell Sci , vol.125 , pp. 531-537
    • Metzger, M.B.1    Hristova, V.A.2    Weissman, A.M.3
  • 129
    • 77954444479 scopus 로고    scopus 로고
    • A HECT E3 ubiquitin ligase negatively regulates Arabidopsis leaf senescence through degradation of the transcription factor WRKY53
    • 10.1111/j.1365-313X.2010.04233.x 1:CAS:528:DC%2BC3cXpslymsr4%3D 20409006
    • Miao Y, Zentgraf U (2010) A HECT E3 ubiquitin ligase negatively regulates Arabidopsis leaf senescence through degradation of the transcription factor WRKY53. Plant J 63:179-188. doi: 10.1111/j.1365-313X.2010.04233.x
    • (2010) Plant J , vol.63 , pp. 179-188
    • Miao, Y.1    Zentgraf, U.2
  • 130
    • 67449091213 scopus 로고    scopus 로고
    • What was the set of ubiquitin and ubiquitin-like conjugating enzymes in the eukaryote common ancestor?
    • 10.1007/s00239-009-9225-6 1:CAS:528:DC%2BD1MXmvV2rsL8%3D 19452197
    • Michelle C, Vourc'h P, Mignon L, Andres CR (2009) What was the set of ubiquitin and ubiquitin-like conjugating enzymes in the eukaryote common ancestor? J Mol Evol 68:616-628. doi: 10.1007/s00239-009-9225-6
    • (2009) J Mol Evol , vol.68 , pp. 616-628
    • Michelle, C.1    Vourc'H, P.2    Mignon, L.3    Andres, C.R.4
  • 134
    • 33845609865 scopus 로고    scopus 로고
    • Mutual antagonism of target of rapamycin and calcineurin signaling
    • 10.1074/jbc.M604244200 1:CAS:528:DC%2BD28XhtFegsLnL 16959779
    • Mulet JM, Martin DE, Loewith R, Hall MN (2006) Mutual antagonism of target of rapamycin and calcineurin signaling. J Biol Chem 281:33000-33007. doi: 10.1074/jbc.M604244200
    • (2006) J Biol Chem , vol.281 , pp. 33000-33007
    • Mulet, J.M.1    Martin, D.E.2    Loewith, R.3    Hall, M.N.4
  • 137
    • 77955058247 scopus 로고    scopus 로고
    • Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase to mediate ubiquitination of the beta2-adrenergic receptor
    • 10.1038/embor.2010.80 1:CAS:528:DC%2BC3cXnsFKiurc%3D 20559325
    • Nabhan JF, Pan H, Lu Q (2010) Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase to mediate ubiquitination of the beta2-adrenergic receptor. EMBO Rep 11:605-611. doi: 10.1038/embor.2010.80
    • (2010) EMBO Rep , vol.11 , pp. 605-611
    • Nabhan, J.F.1    Pan, H.2    Lu, Q.3
  • 138
    • 0000693801 scopus 로고    scopus 로고
    • Internalization and recycling of the C5a anaphylatoxin receptor: Evidence that the agonist-mediated internalization is modulated by phosphorylation of the C-terminal domain
    • 1:CAS:528:DyaK2sXnt1Gitbc%3D 9410877
    • Naik N, Giannini E, Brouchon L, Boulay F (1997) Internalization and recycling of the C5a anaphylatoxin receptor: evidence that the agonist-mediated internalization is modulated by phosphorylation of the C-terminal domain. J Cell Sci 110(Pt 19):2381-2390
    • (1997) J Cell Sci , vol.110 , Issue.PART 19 , pp. 2381-2390
    • Naik, N.1    Giannini, E.2    Brouchon, L.3    Boulay, F.4
  • 139
    • 12544258841 scopus 로고    scopus 로고
    • + exchanger isoforms are distributed to Golgi and post-Golgi compartments and are involved in organelle pH regulation
    • 10.1074/jbc.M410041200 1:CAS:528:DC%2BD2MXitFCrug%3D%3D 15522866
    • + exchanger isoforms are distributed to Golgi and post-Golgi compartments and are involved in organelle pH regulation. J Biol Chem 280:1561-1572. doi: 10.1074/jbc.M410041200
    • (2005) J Biol Chem , vol.280 , pp. 1561-1572
    • Nakamura, N.1    Tanaka, S.2    Teko, Y.3    Mitsui, K.4    Kanazawa, H.5
  • 140
    • 0032516911 scopus 로고    scopus 로고
    • + exchanger in a late endosomal compartment of yeast. Implications for vacuole biogenesis
    • 1:CAS:528:DyaK1cXlsFOrsL0%3D 9694857
    • + exchanger in a late endosomal compartment of yeast. Implications for vacuole biogenesis. J Biol Chem 273:21054-21060
    • (1998) J Biol Chem , vol.273 , pp. 21054-21060
    • Nass, R.1    Rao, R.2
  • 141
    • 0030704674 scopus 로고    scopus 로고
    • +-ATPase. Insights into mechanisms of sodium tolerance
    • 1:CAS:528:DyaK2sXmvV2jurs%3D 9334180
    • +-ATPase. Insights into mechanisms of sodium tolerance. J Biol Chem 272:26145-26152
    • (1997) J Biol Chem , vol.272 , pp. 26145-26152
    • Nass, R.1    Cunningham, K.W.2    Rao, R.3
  • 142
    • 77954480051 scopus 로고    scopus 로고
    • Lack of main K plus uptake systems in Saccharomyces cerevisiae cells affects yeast performance in both potassium-sufficient and potassium-limiting conditions
    • 10.1111/j.1567-1364.2010.00630.x 1:CAS:528:DC%2BC3cXpvVOntLc%3D 20491939
    • Navarrete C, Petrezselyova S, Barreto L, Martinez JL, Zahradka J, Arino J, Sychrova H, Ramos J (2010) Lack of main K plus uptake systems in Saccharomyces cerevisiae cells affects yeast performance in both potassium-sufficient and potassium-limiting conditions. FEMS Yeast Res 10:508-517. doi: 10.1111/j.1567-1364.2010.00630.x
    • (2010) FEMS Yeast Res , vol.10 , pp. 508-517
    • Navarrete, C.1    Petrezselyova, S.2    Barreto, L.3    Martinez, J.L.4    Zahradka, J.5    Arino, J.6    Sychrova, H.7    Ramos, J.8
  • 143
    • 33845317263 scopus 로고    scopus 로고
    • Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes
    • 10.1083/jcb.200606113 1:CAS:528:DC%2BD28XhtlWgt7jP 17130288
    • Nickerson DP, West M, Odorizzi G (2006) Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes. J Cell Biol 175:715-720. doi: 10.1083/jcb.200606113
    • (2006) J Cell Biol , vol.175 , pp. 715-720
    • Nickerson, D.P.1    West, M.2    Odorizzi, G.3
  • 144
    • 28344456279 scopus 로고    scopus 로고
    • A genomic and functional inventory of deubiquitinating enzymes
    • 10.1016/j.cell.2005.11.007 1:CAS:528:DC%2BD2MXhtlWntLjP 16325574
    • Nijman SM, Luna-Vargas MP, Velds A, Brummelkamp TR, Dirac AM, Sixma TK, Bernards R (2005) A genomic and functional inventory of deubiquitinating enzymes. Cell 123:773-786. doi: 10.1016/j.cell.2005.11.007
    • (2005) Cell , vol.123 , pp. 773-786
    • Nijman, S.M.1    Luna-Vargas, M.P.2    Velds, A.3    Brummelkamp, T.R.4    Dirac, A.M.5    Sixma, T.K.6    Bernards, R.7
  • 145
    • 70649112359 scopus 로고    scopus 로고
    • Arrestin-mediated endocytosis of yeast plasma membrane transporters
    • 10.1111/j.1600-0854.2009.00990.x 1:CAS:528:DC%2BD1MXhsFajsbvJ 19912579
    • Nikko E, Pelham HR (2009) Arrestin-mediated endocytosis of yeast plasma membrane transporters. Traffic 10:1856-1867. doi: 10.1111/j.1600-0854.2009. 00990.x
    • (2009) Traffic , vol.10 , pp. 1856-1867
    • Nikko, E.1    Pelham, H.R.2
  • 146
    • 57049101734 scopus 로고    scopus 로고
    • Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1
    • 10.1038/embor.2008.199 1:CAS:528:DC%2BD1cXhsVWgsr%2FF 18953286
    • Nikko E, Sullivan JA, Pelham HR (2008) Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1. EMBO Rep 9:1216-1221. doi: 10.1038/embor.2008.199
    • (2008) EMBO Rep , vol.9 , pp. 1216-1221
    • Nikko, E.1    Sullivan, J.A.2    Pelham, H.R.3
  • 148
    • 35148831808 scopus 로고    scopus 로고
    • Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4
    • 10.1038/nature06171 1:CAS:528:DC%2BD2sXhtFChu77N 17928861
    • Obita T, Saksena S, Ghazi-Tabatabai S, Gill DJ, Perisic O, Emr SD, Williams RL (2007) Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4. Nature 449:735-739. doi: 10.1038/nature06171
    • (2007) Nature , vol.449 , pp. 735-739
    • Obita, T.1    Saksena, S.2    Ghazi-Tabatabai, S.3    Gill, D.J.4    Perisic, O.5    Emr, S.D.6    Williams, R.L.7
  • 149
    • 33845386442 scopus 로고    scopus 로고
    • Ndfip1 protein promotes the function of itch ubiquitin ligase to prevent T cell activation and T helper 2 cell-mediated inflammation
    • 10.1016/j.immuni.2006.10.012 1:CAS:528:DC%2BD2sXisFeitA%3D%3D 17137798
    • Oliver PM, Cao X, Worthen GS, Shi P, Briones N, MacLeod M, White J, Kirby P, Kappler J, Marrack P, Yang B (2006) Ndfip1 protein promotes the function of itch ubiquitin ligase to prevent T cell activation and T helper 2 cell-mediated inflammation. Immunity 25:929-940. doi: 10.1016/j.immuni.2006.10.012
    • (2006) Immunity , vol.25 , pp. 929-940
    • Oliver, P.M.1    Cao, X.2    Worthen, G.S.3    Shi, P.4    Briones, N.5    Macleod, M.6    White, J.7    Kirby, P.8    Kappler, J.9    Marrack, P.10    Yang, B.11
  • 150
    • 79959365769 scopus 로고    scopus 로고
    • Plant science. Innate immunity in plants goes to the PUB
    • 10.1126/science.1208448 21680829
    • O'Neill LA (2011) Plant science. Innate immunity in plants goes to the PUB. Science 332:1386-1387. doi: 10.1126/science.1208448
    • (2011) Science , vol.332 , pp. 1386-1387
    • O'Neill, L.A.1
  • 152
    • 51849153334 scopus 로고    scopus 로고
    • Endosomal functions in plants
    • 10.1111/j.1600-0854.2008.00787.x 1:CAS:528:DC%2BD1cXht1GlsrnM 18627577
    • Otegui MS, Spitzer C (2008) Endosomal functions in plants. Traffic 9:1589-1598. doi: 10.1111/j.1600-0854.2008.00787.x
    • (2008) Traffic , vol.9 , pp. 1589-1598
    • Otegui, M.S.1    Spitzer, C.2
  • 153
    • 0031009124 scopus 로고    scopus 로고
    • Two homologous phosphorylation domains differentially contribute to desensitization and internalization of the m2 muscarinic acetylcholine receptor
    • 1:CAS:528:DyaK2sXjsFOjurk%3D 9162044
    • Pals-Rylaarsdam R, Hosey MM (1997) Two homologous phosphorylation domains differentially contribute to desensitization and internalization of the m2 muscarinic acetylcholine receptor. J Biol Chem 272:14152-14158
    • (1997) J Biol Chem , vol.272 , pp. 14152-14158
    • Pals-Rylaarsdam, R.1    Hosey, M.M.2
  • 156
    • 84876691421 scopus 로고    scopus 로고
    • Ubiquitin protein ligase 3 mediates the proteasomal degradation of GLABROUS 3 and ENHANCER of GLABROUS 3, regulators of trichome development and flavonoid biosynthesis in Arabidopsis
    • 10.1111/tpj.12132 1:CAS:528:DC%2BC3sXmtlWnt7w%3D 23373825
    • Patra B, Pattanaik S, Yuan L (2013) Ubiquitin protein ligase 3 mediates the proteasomal degradation of GLABROUS 3 and ENHANCER OF GLABROUS 3, regulators of trichome development and flavonoid biosynthesis in Arabidopsis. Plant J 74:435-447. doi: 10.1111/tpj.12132
    • (2013) Plant J , vol.74 , pp. 435-447
    • Patra, B.1    Pattanaik, S.2    Yuan, L.3
  • 157
    • 84860355658 scopus 로고    scopus 로고
    • An expanded family of arrestins regulate metabolism
    • 10.1016/j.tem.2012.03.003 1:CAS:528:DC%2BC38XlvVSgs7w%3D 22520962
    • Patwari P, Lee RT (2012) An expanded family of arrestins regulate metabolism. Trends Endocrinol Metab 23:216-222. doi: 10.1016/j.tem.2012.03.003
    • (2012) Trends Endocrinol Metab , vol.23 , pp. 216-222
    • Patwari, P.1    Lee, R.T.2
  • 158
    • 69949139700 scopus 로고    scopus 로고
    • Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins
    • 10.1074/jbc.M109.018093 1:CAS:528:DC%2BD1MXhtV2nsLbK 19605364
    • Patwari P, Chutkow WA, Cummings K, Verstraeten VL, Lammerding J, Schreiter ER, Lee RT (2009) Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins. J Biol Chem 284:24996-25003. doi: 10.1074/jbc.M109.018093
    • (2009) J Biol Chem , vol.284 , pp. 24996-25003
    • Patwari, P.1    Chutkow, W.A.2    Cummings, K.3    Verstraeten, V.L.4    Lammerding, J.5    Schreiter, E.R.6    Lee, R.T.7
  • 159
    • 70350322311 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression
    • 10.1128/JVI.00574-09 1:CAS:528:DC%2BD1MXhsVSmtL%2FK 19692479
    • Pawliczek T, Crump CM (2009) Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression. J Virol 83:11254-11264. doi: 10.1128/JVI.00574-09
    • (2009) J Virol , vol.83 , pp. 11254-11264
    • Pawliczek, T.1    Crump, C.M.2
  • 160
    • 79960034065 scopus 로고    scopus 로고
    • Plasma membrane protein trafficking
    • A. Murphy W. Peer B. Schultz (eds) Springer-Verlag Berlin
    • Peer WA (2011) Plasma membrane protein trafficking. In: Murphy A, Peer W, Schultz B (eds) The plant plasma membrane. Springer-Verlag, Berlin, pp 31-56
    • (2011) The Plant Plasma Membrane , pp. 31-56
    • Peer, W.A.1
  • 163
  • 164
    • 0035854747 scopus 로고    scopus 로고
    • Anti-apoptotic signaling of the insulin-like growth factor-I receptor through mitochondrial translocation of c-Raf and Nedd4
    • 10.1074/jbc.M103188200 1:CAS:528:DC%2BD3MXlsVKgu7s%3D 11352919
    • Peruzzi F, Prisco M, Morrione A, Valentinis B, Baserga R (2001) Anti-apoptotic signaling of the insulin-like growth factor-I receptor through mitochondrial translocation of c-Raf and Nedd4. J Biol Chem 276:25990-25996. doi: 10.1074/jbc.M103188200
    • (2001) J Biol Chem , vol.276 , pp. 25990-25996
    • Peruzzi, F.1    Prisco, M.2    Morrione, A.3    Valentinis, B.4    Baserga, R.5
  • 165
    • 42949112146 scopus 로고    scopus 로고
    • ESCRT factors restrict mycobacterial growth
    • 10.1073/pnas.0707206105 1:CAS:528:DC%2BD1cXjtVSit7Y%3D 18287038
    • Philips JA, Porto MC, Wang H, Rubin EJ, Perrimon N (2008) ESCRT factors restrict mycobacterial growth. Proc Natl Acad Sci USA 105:3070-3075. doi: 10.1073/pnas.0707206105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3070-3075
    • Philips, J.A.1    Porto, M.C.2    Wang, H.3    Rubin, E.J.4    Perrimon, N.5
  • 166
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • 1:CAS:528:DC%2BD2cXhtValsrg%3D 14744430
    • Pickart CM (2004) Back to the future with ubiquitin. Cell 116:181-190
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 167
    • 2342450002 scopus 로고    scopus 로고
    • Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast
    • 10.1091/mbc.E03-10-0727 1:CAS:528:DC%2BD2cXjvFKjtbw%3D 15020711
    • Pizzirusso M, Chang A (2004) Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast. Mol Biol Cell 15:2401-2409. doi: 10.1091/mbc.E03-10-0727
    • (2004) Mol Biol Cell , vol.15 , pp. 2401-2409
    • Pizzirusso, M.1    Chang, A.2
  • 168
    • 77951918362 scopus 로고    scopus 로고
    • Identification of the switch in early-to-late endosome transition
    • 10.1016/j.cell.2010.03.011 1:CAS:528:DC%2BC3cXlvFygt70%3D 20434987
    • Poteryaev D, Datta S, Ackema K, Zerial M, Spang A (2010) Identification of the switch in early-to-late endosome transition. Cell 141:497-508. doi: 10.1016/j.cell.2010.03.011
    • (2010) Cell , vol.141 , pp. 497-508
    • Poteryaev, D.1    Datta, S.2    Ackema, K.3    Zerial, M.4    Spang, A.5
  • 169
    • 34249674993 scopus 로고    scopus 로고
    • The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitin-dependent sorting
    • 10.1016/j.devcel.2007.04.013 1:CAS:528:DC%2BD2sXmsFentrk%3D 17543868
    • Prag G, Watson H, Kim YC, Beach BM, Ghirlando R, Hummer G, Bonifacino JS, Hurley JH (2007) The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitin-dependent sorting. Dev Cell 12:973-986. doi: 10.1016/j.devcel.2007.04. 013
    • (2007) Dev Cell , vol.12 , pp. 973-986
    • Prag, G.1    Watson, H.2    Kim, Y.C.3    Beach, B.M.4    Ghirlando, R.5    Hummer, G.6    Bonifacino, J.S.7    Hurley, J.H.8
  • 170
    • 77956912124 scopus 로고    scopus 로고
    • + exchanger Nhx1p regulates the initiation of Saccharomyces cerevisiae vacuole fusion
    • 10.1242/jcs.067637 1:CAS:528:DC%2BC3cXhsFGgur%2FM 20826459
    • + exchanger Nhx1p regulates the initiation of Saccharomyces cerevisiae vacuole fusion. J Cell Sci 123:3266-3275. doi: 10.1242/jcs.067637
    • (2010) J Cell Sci , vol.123 , pp. 3266-3275
    • Qiu, Q.S.1    Fratti, R.A.2
  • 171
    • 79952298500 scopus 로고    scopus 로고
    • Activation of the plasma membrane Na/H antiporter Salt-Overly-Sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
    • 10.1073/pnas.1018921108 1:CAS:528:DC%2BC3MXitFemsbY%3D 21262798
    • Quintero FJ, Martinez-Atienza J, Villalta I, Jiang X, Kim WY, Ali Z, Fujii H, Mendoza I, Yun DJ, Zhu JK, Pardo JM (2011) Activation of the plasma membrane Na/H antiporter Salt-Overly-Sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain. Proc Natl Acad Sci USA 108:2611-2616. doi: 10.1073/pnas.1018921108
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 2611-2616
    • Quintero, F.J.1    Martinez-Atienza, J.2    Villalta, I.3    Jiang, X.4    Kim, W.Y.5    Ali, Z.6    Fujii, H.7    Mendoza, I.8    Yun, D.J.9    Zhu, J.K.10    Pardo, J.M.11
  • 172
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class e vps mutants
    • 1:CAS:528:DyaK3sXhvVOlsLw%3D 1493335
    • Raymond CK, Howald-Stevenson I, Vater CA, Stevens TH (1992) Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol Biol Cell 3:1389-1402
    • (1992) Mol Biol Cell , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 173
    • 12344250580 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B
    • 10.1093/hmg/ddi003 1:CAS:528:DC%2BD2MXitFGmsA%3D%3D 15537668
    • Reid E, Connell J, Edwards TL, Duley S, Brown SE, Sanderson CM (2005) The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B. Hum Mol Genet 14:19-38. doi: 10.1093/hmg/ddi003
    • (2005) Hum Mol Genet , vol.14 , pp. 19-38
    • Reid, E.1    Connell, J.2    Edwards, T.L.3    Duley, S.4    Brown, S.E.5    Sanderson, C.M.6
  • 174
    • 83055172985 scopus 로고    scopus 로고
    • Plant endosomal trafficking pathways
    • 10.1016/j.pbi.2011.07.009 1:CAS:528:DC%2BC3MXhsFygu7vO 21821464
    • Reyes FC, Buono R, Otegui MS (2011) Plant endosomal trafficking pathways. Curr Opin Plant Biol 14:666-673. doi: 10.1016/j.pbi.2011.07.009
    • (2011) Curr Opin Plant Biol , vol.14 , pp. 666-673
    • Reyes, F.C.1    Buono, R.2    Otegui, M.S.3
  • 175
    • 33644780918 scopus 로고    scopus 로고
    • Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis
    • 10.1101/gad.366506 1:CAS:528:DC%2BD28Xit1Kmtb8%3D 16510871
    • Robatzek S, Chinchilla D, Boller T (2006) Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis. Genes Dev 20:537-542. doi: 10.1101/gad.366506
    • (2006) Genes Dev , vol.20 , pp. 537-542
    • Robatzek, S.1    Chinchilla, D.2    Boller, T.3
  • 176
    • 0030990121 scopus 로고    scopus 로고
    • Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae
    • 1:CAS:528:DyaK2sXkt1yisr8%3D 9199164
    • Roberg KJ, Rowley N, Kaiser CA (1997) Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae. J Cell Biol 137:1469-1482
    • (1997) J Cell Biol , vol.137 , pp. 1469-1482
    • Roberg, K.J.1    Rowley, N.2    Kaiser, C.A.3
  • 177
    • 0042812051 scopus 로고    scopus 로고
    • The HECT ubiquitin ligase Rsp5p is required for proper nuclear export of mRNA in Saccharomyces cerevisiae
    • 1:CAS:528:DC%2BD3sXlvVyjtLo%3D 12839499
    • Rodriguez MS, Gwizdek C, Haguenauer-Tsapis R, Dargemont C (2003) The HECT ubiquitin ligase Rsp5p is required for proper nuclear export of mRNA in Saccharomyces cerevisiae. Traffic 4:566-575
    • (2003) Traffic , vol.4 , pp. 566-575
    • Rodriguez, M.S.1    Gwizdek, C.2    Haguenauer-Tsapis, R.3    Dargemont, C.4
  • 181
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • 10.1038/nrm2690 1:CAS:528:DC%2BD1MXlslGntbw%3D 19436320
    • Rotin D, Kumar S (2009) Physiological functions of the HECT family of ubiquitin ligases. Nat Rev Mol Cell Biol 10:398-409. doi: 10.1038/nrm2690
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 182
    • 0034235434 scopus 로고    scopus 로고
    • Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/Rsp5p family of ubiquitin-protein ligases
    • 1:CAS:528:DC%2BD3cXkvFCktLo%3D 10882424
    • Rotin D, Staub O, Haguenauer-Tsapis R (2000) Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases. J Membr Biol 176:1-17
    • (2000) J Membr Biol , vol.176 , pp. 1-17
    • Rotin, D.1    Staub, O.2    Haguenauer-Tsapis, R.3
  • 184
    • 39449140052 scopus 로고    scopus 로고
    • Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting
    • 10.1091/mbc.E07-07-0694 1:CAS:528:DC%2BD1cXlslentLo%3D 18032584
    • Rue SM, Mattei S, Saksena S, Emr SD (2008) Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting. Mol Biol Cell 19:475-484. doi: 10.1091/mbc.E07-07-0694
    • (2008) Mol Biol Cell , vol.19 , pp. 475-484
    • Rue, S.M.1    Mattei, S.2    Saksena, S.3    Emr, S.D.4
  • 185
    • 58149103425 scopus 로고    scopus 로고
    • Functional reconstitution of ESCRT-III assembly and disassembly
    • 10.1016/j.cell.2008.11.013 1:CAS:528:DC%2BD1MXhtFOisbY%3D 19135892
    • Saksena S, Wahlman J, Teis D, Johnson AE, Emr SD (2009) Functional reconstitution of ESCRT-III assembly and disassembly. Cell 136:97-109. doi: 10.1016/j.cell.2008.11.013
    • (2009) Cell , vol.136 , pp. 97-109
    • Saksena, S.1    Wahlman, J.2    Teis, D.3    Johnson, A.E.4    Emr, S.D.5
  • 186
    • 58149230938 scopus 로고    scopus 로고
    • A role for the ESCRT system in cell division in archaea
    • 10.1126/science.1165322 1:CAS:528:DC%2BD1cXhsVOgtbvK 19008417
    • Samson RY, Obita T, Freund SM, Williams RL, Bell SD (2008) A role for the ESCRT system in cell division in archaea. Science 322:1710-1713. doi: 10.1126/science.1165322
    • (2008) Science , vol.322 , pp. 1710-1713
    • Samson, R.Y.1    Obita, T.2    Freund, S.M.3    Williams, R.L.4    Bell, S.D.5
  • 187
    • 84878347483 scopus 로고    scopus 로고
    • Phosphorylation of a conserved Thr357 in yeast Nedd4-like ubiquitin ligase Rsp5 is involved in down-regulation of the general amino acid permease Gap1
    • 10.1111/gtc.12049
    • Sasaki T, Takagi H (2013) Phosphorylation of a conserved Thr357 in yeast Nedd4-like ubiquitin ligase Rsp5 is involved in down-regulation of the general amino acid permease Gap1. Genes Cells. doi: 10.1111/gtc.12049
    • (2013) Genes Cells
    • Sasaki, T.1    Takagi, H.2
  • 188
    • 0027099840 scopus 로고
    • Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNA
    • 1:CAS:528:DyaK3sXltlaksQ%3D%3D 8966547
    • Schachtman DP, Schroeder JI, Lucas WJ, Anderson JA, Gaber RF (1992) Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNA. Science 258:1654-1658
    • (1992) Science , vol.258 , pp. 1654-1658
    • Schachtman, D.P.1    Schroeder, J.I.2    Lucas, W.J.3    Anderson, J.A.4    Gaber, R.F.5
  • 189
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • 1:CAS:528:DyaK2cXlvFKm 8221889
    • Scheffner M, Huibregtse JM, Vierstra RD, Howley PM (1993) The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75:495-505
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 190
    • 70450250211 scopus 로고    scopus 로고
    • Coats of endosomal protein sorting: Retromer and ESCRT
    • 10.1016/j.pbi.2009.09.005 1:CAS:528:DC%2BD1MXhsV2murjL 19836992
    • Schellmann S, Pimpl P (2009) Coats of endosomal protein sorting: retromer and ESCRT. Curr Opin Plant Biol 12:670-676. doi: 10.1016/j.pbi.2009.09.005
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 670-676
    • Schellmann, S.1    Pimpl, P.2
  • 191
    • 52749089159 scopus 로고    scopus 로고
    • Regulation of the voltage-gated K(+) channels KCNQ2/3 and KCNQ3/5 by serum- and glucocorticoid-regulated kinase-1
    • 10.1152/ajpcell.00146.2008 1:CAS:528:DC%2BD1cXoslyhtr8%3D 18463232
    • Schuetz F, Kumar S, Poronnik P, Adams DJ (2008) Regulation of the voltage-gated K(+) channels KCNQ2/3 and KCNQ3/5 by serum- and glucocorticoid-regulated kinase-1. Am J Physiol Cell Physiol 295:C73-C80. doi: 10.1152/ajpcell.00146.2008
    • (2008) Am J Physiol Cell Physiol , vol.295
    • Schuetz, F.1    Kumar, S.2    Poronnik, P.3    Adams, D.J.4
  • 192
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signalling pathways
    • 10.1038/nrm2673 1:CAS:528:DC%2BD1MXktFGrsL8%3D 19352404
    • Schulman BA, Harper JW (2009) Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nat Rev Mol Cell Biol 10:319-331. doi: 10.1038/nrm2673
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 193
    • 42549168016 scopus 로고    scopus 로고
    • Functional expression of the voltage-gated neuronal mammalian potassium channel rat ether à go-go1 in yeast
    • 10.1111/j.1567-1364.2007.00351.x 1:CAS:528:DC%2BD1cXlvVKntbY%3D 18248412
    • Schwarzer S, Kolacna L, Lichtenberg-Fraté H, Sychrova H, Ludwig J (2008) Functional expression of the voltage-gated neuronal mammalian potassium channel rat ether à go-go1 in yeast. FEMS Yeast Res 8:405-413. doi: 10.1111/j.1567-1364.2007.00351.x
    • (2008) FEMS Yeast Res , vol.8 , pp. 405-413
    • Schwarzer, S.1    Kolacna, L.2    Lichtenberg-Fraté, H.3    Sychrova, H.4    Ludwig, J.5
  • 195
    • 0038376459 scopus 로고    scopus 로고
    • Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90
    • 1:CAS:528:DC%2BD3sXls1Olsbk%3D 12867034
    • Shcherbik N, Zoladek T, Nickels JT, Haines DS (2003) Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90. Curr Biol 13:1227-1233
    • (2003) Curr Biol , vol.13 , pp. 1227-1233
    • Shcherbik, N.1    Zoladek, T.2    Nickels, J.T.3    Haines, D.S.4
  • 196
    • 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
    • 10.1074/jbc.M410325200 1:CAS:528:DC%2BD2cXhtVKqu7vL 15466864
    • Shcherbik N, Kee Y, Lyon N, Huibregtse JM, Haines DS (2004) 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 279:53892-53898. doi: 10.1074/jbc.M410325200
    • (2004) J Biol Chem , vol.279 , pp. 53892-53898
    • Shcherbik, N.1    Kee, Y.2    Lyon, N.3    Huibregtse, J.M.4    Haines, D.S.5
  • 197
    • 84870879702 scopus 로고    scopus 로고
    • Mammalian alpha arrestins link activated seven transmembrane receptors to Nedd4 family e3 ubiquitin ligases and interact with beta arrestins
    • 10.1371/journal.pone.0050557 1:CAS:528:DC%2BC38XhvV2qsbrK 23236378
    • Shea FF, Rowell JL, Li Y, Chang TH, Alvarez CE (2012) Mammalian alpha arrestins link activated seven transmembrane receptors to Nedd4 family e3 ubiquitin ligases and interact with beta arrestins. PLoS ONE 7:e50557. doi: 10.1371/journal.pone.0050557
    • (2012) PLoS ONE , vol.7 , pp. 50557
    • Shea, F.F.1    Rowell, J.L.2    Li, Y.3    Chang, T.H.4    Alvarez, C.E.5
  • 198
    • 33745089231 scopus 로고    scopus 로고
    • Regulation of functional diversity within the Nedd4 family by accessory and adaptor proteins
    • 10.1002/bies.20422 1:CAS:528:DC%2BD28XmtFKmtrk%3D 16700065
    • Shearwin-Whyatt L, Dalton HE, Foot N, Kumar S (2006) Regulation of functional diversity within the Nedd4 family by accessory and adaptor proteins. BioEssays 28:617-628. doi: 10.1002/bies.20422
    • (2006) BioEssays , vol.28 , pp. 617-628
    • Shearwin-Whyatt, L.1    Dalton, H.E.2    Foot, N.3    Kumar, S.4
  • 199
    • 0038657685 scopus 로고    scopus 로고
    • Sal1 determines the number of aleurone cell layers in maize endosperm and encodes a class e vacuolar sorting protein
    • 10.1073/pnas.0732023100 1:CAS:528:DC%2BD3sXktlyhu7s%3D 12750475
    • Shen B, Li C, Min Z, Meeley RB, Tarczynski MC, Olsen OA (2003) sal1 determines the number of aleurone cell layers in maize endosperm and encodes a class E vacuolar sorting protein. Proc Natl Acad Sci USA 100:6552-6557. doi: 10.1073/pnas.0732023100
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6552-6557
    • Shen, B.1    Li, C.2    Min, Z.3    Meeley, R.B.4    Tarczynski, M.C.5    Olsen, O.A.6
  • 201
  • 203
    • 38449117567 scopus 로고    scopus 로고
    • Involvement of vacuolar protein sorting pathway in Ebola virus release independent of TSG101 interaction
    • 10.1086/520610 1:CAS:528:DC%2BD2sXhsVamsr7F 17940959
    • Silvestri LS, Ruthel G, Kallstrom G, Warfield KL, Swenson DL, Nelle T, Iversen PL, Bavari S, Aman MJ (2007) Involvement of vacuolar protein sorting pathway in Ebola virus release independent of TSG101 interaction. J Infect Dis 196(Suppl 2):S264-S270. doi: 10.1086/520610
    • (2007) J Infect Dis , vol.196 , Issue.SUPPL. 2
    • Silvestri, L.S.1    Ruthel, G.2    Kallstrom, G.3    Warfield, K.L.4    Swenson, D.L.5    Nelle, T.6    Iversen, P.L.7    Bavari, S.8    Aman, M.J.9
  • 206
    • 1042278123 scopus 로고    scopus 로고
    • Relative contribution of Nedd4 and Nedd4-2 to ENaC regulation in epithelia determined by RNA interference
    • 10.1074/jbc.M312477200 1:CAS:528:DC%2BD2cXpslSiug%3D%3D 14645220
    • Snyder PM, Steines JC, Olson DR (2004) Relative contribution of Nedd4 and Nedd4-2 to ENaC regulation in epithelia determined by RNA interference. J Biol Chem 279:5042-5046. doi: 10.1074/jbc.M312477200
    • (2004) J Biol Chem , vol.279 , pp. 5042-5046
    • Snyder, P.M.1    Steines, J.C.2    Olson, D.R.3
  • 208
    • 66449089453 scopus 로고    scopus 로고
    • The ESCRT-related CHMP1A and B proteins mediate multivesicular body sorting of auxin carriers in Arabidopsis and are required for plant development
    • 10.1105/tpc.108.064865 1:CAS:528:DC%2BD1MXlsFyltbs%3D 19304934
    • Spitzer C, Reyes FC, Buono R, Sliwinski MK, Haas TJ, Otegui MS (2009) The ESCRT-related CHMP1A and B proteins mediate multivesicular body sorting of auxin carriers in Arabidopsis and are required for plant development. Plant Cell 21:749-766. doi: 10.1105/tpc.108.064865
    • (2009) Plant Cell , vol.21 , pp. 749-766
    • Spitzer, C.1    Reyes, F.C.2    Buono, R.3    Sliwinski, M.K.4    Haas, T.J.5    Otegui, M.S.6
  • 210
    • 0034916615 scopus 로고    scopus 로고
    • CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression
    • 1:CAS:528:DC%2BD3MXlsFamtL8%3D 11559747
    • Stauffer DR, Howard TL, Nyun T, Hollenberg SM (2001) CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression. J Cell Sci 114:2383-2393
    • (2001) J Cell Sci , vol.114 , pp. 2383-2393
    • Stauffer, D.R.1    Howard, T.L.2    Nyun, T.3    Hollenberg, S.M.4
  • 211
    • 34347379169 scopus 로고    scopus 로고
    • Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase rsp5 to membrane proteins in vivo and in vitro
    • 10.1091/mbc.E07-01-0011 1:CAS:528:DC%2BD2sXnsVWqtr4%3D 17429078
    • Sullivan JA, Lewis MJ, Nikko E, Pelham HR (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. doi: 10.1091/mbc.E07-01-0011
    • (2007) Mol Biol Cell , vol.18 , pp. 2429-2440
    • Sullivan, J.A.1    Lewis, M.J.2    Nikko, E.3    Pelham, H.R.4
  • 213
    • 0037044788 scopus 로고    scopus 로고
    • + exchanger NHE5 isoform. Regulation by phosphatidylinositol 3′-kinase and the actin cytoskeleton
    • 10.1074/jbc.M206629200 1:CAS:528:DC%2BD38Xos1ensbg%3D 12205089
    • + exchanger NHE5 isoform. Regulation by phosphatidylinositol 3′-kinase and the actin cytoskeleton. J Biol Chem 277:42623-42632. doi: 10.1074/jbc.M206629200
    • (2002) J Biol Chem , vol.277 , pp. 42623-42632
    • Szaszi, K.1    Paulsen, A.2    Szabo, E.Z.3    Numata, M.4    Grinstein, S.5    Orlowski, J.6
  • 214
    • 65349109163 scopus 로고    scopus 로고
    • A simple and high-sensitivity method for analysis of ubiquitination and polyubiquitination based on wheat cell-free protein synthesis
    • 10.1186/1471-2229-9-39 19348673
    • Takahashi H, Nozawa A, Seki M, Shinozaki K, Endo Y, Sawasaki T (2009) A simple and high-sensitivity method for analysis of ubiquitination and polyubiquitination based on wheat cell-free protein synthesis. BMC Plant Biol 9:39. doi: 10.1186/1471-2229-9-39
    • (2009) BMC Plant Biol , vol.9 , pp. 39
    • Takahashi, H.1    Nozawa, A.2    Seki, M.3    Shinozaki, K.4    Endo, Y.5    Sawasaki, T.6
  • 215
    • 24744469420 scopus 로고    scopus 로고
    • Endocytosis and degradation of BOR1, a boron transporter of Arabidopsis thaliana, regulated by boron availability
    • 10.1073/pnas.0502060102 1:CAS:528:DC%2BD2MXps1yqsb8%3D 16103374
    • Takano J, Miwa K, Yuan L, von Wirén N, Fujiwara T (2005) Endocytosis and degradation of BOR1, a boron transporter of Arabidopsis thaliana, regulated by boron availability. Proc Natl Acad Sci USA 102:12276-12281. doi: 10.1073/pnas.0502060102
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12276-12281
    • Takano, J.1    Miwa, K.2    Yuan, L.3    Von Wirén, N.4    Fujiwara, T.5
  • 216
    • 77950424657 scopus 로고    scopus 로고
    • Polar localization and degradation of Arabidopsis boron transporters through distinct trafficking pathways
    • 10.1073/pnas.0910744107 1:CAS:528:DC%2BC3cXjvFemu7k%3D 20194745
    • Takano J, Tanaka M, Toyoda A, Miwa K, Kasai K, Fuji K, Onouchi H, Naito S, Fujiwara T (2010) Polar localization and degradation of Arabidopsis boron transporters through distinct trafficking pathways. Proc Natl Acad Sci USA 107:5220-5225. doi: 10.1073/pnas.0910744107
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5220-5225
    • Takano, J.1    Tanaka, M.2    Toyoda, A.3    Miwa, K.4    Kasai, K.5    Fuji, K.6    Onouchi, H.7    Naito, S.8    Fujiwara, T.9
  • 218
    • 53249131094 scopus 로고    scopus 로고
    • Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation
    • 10.1016/j.devcel.2008.08.013 1:CAS:528:DC%2BD1cXht1ymu7vM 18854142
    • Teis D, Saksena S, Emr SD (2008) Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation. Dev Cell 15:578-589. doi: 10.1016/j.devcel.2008.08.013
    • (2008) Dev Cell , vol.15 , pp. 578-589
    • Teis, D.1    Saksena, S.2    Emr, S.D.3
  • 219
    • 84872801028 scopus 로고    scopus 로고
    • Non-26S proteasome proteolytic role of ubiquitin in plant endocytosis and endosomal trafficking(F)
    • 10.1111/jipb.12007 1:CAS:528:DC%2BC3sXjvFWnsbo%3D 23137267
    • Tian M, Xie Q (2013) Non-26S proteasome proteolytic role of ubiquitin in plant endocytosis and endosomal trafficking(F). J Integr Plant Biol 55:54-63. doi: 10.1111/jipb.12007
    • (2013) J Integr Plant Biol , vol.55 , pp. 54-63
    • Tian, M.1    Xie, Q.2
  • 220
    • 37249034156 scopus 로고    scopus 로고
    • Subcellular localization and functional domain studies of DEFECTIVE KERNEL1 in maize and Arabidopsis suggest a model for aleurone cell fate specification involving CRINKLY4 and SUPERNUMERARY ALEURONE LAYER1
    • 10.1105/tpc.106.048868 1:CAS:528:DC%2BD2sXhsVersLnE 17933905
    • Tian Q, Olsen L, Sun B, Lid SE, Brown RC, Lemmon BE, Fosnes K, Gruis DF, Opsahl-Sorteberg HG, Otegui MS, Olsen OA (2007) Subcellular localization and functional domain studies of DEFECTIVE KERNEL1 in maize and Arabidopsis suggest a model for aleurone cell fate specification involving CRINKLY4 and SUPERNUMERARY ALEURONE LAYER1. Plant Cell 19:3127-3145. doi: 10.1105/tpc.106.048868
    • (2007) Plant Cell , vol.19 , pp. 3127-3145
    • Tian, Q.1    Olsen, L.2    Sun, B.3    Lid, S.E.4    Brown, R.C.5    Lemmon, B.E.6    Fosnes, K.7    Gruis, D.F.8    Opsahl-Sorteberg, H.G.9    Otegui, M.S.10    Olsen, O.A.11
  • 221
    • 34347205268 scopus 로고    scopus 로고
    • Inhibition of tumor growth and metastasis by depletion of vesicular sorting protein Hrs: Its regulatory role on E-cadherin and beta-catenin
    • 10.1158/0008-5472.CAN-06-2756 1:CAS:528:DC%2BD2sXmtVaisb8%3D 17545595
    • Toyoshima M, Tanaka N, Aoki J, Tanaka Y, Murata K, Kyuuma M, Kobayashi H, Ishii N, Yaegashi N, Sugamura K (2007) Inhibition of tumor growth and metastasis by depletion of vesicular sorting protein Hrs: its regulatory role on E-cadherin and beta-catenin. Cancer Res 67:5162-5171. doi: 10.1158/0008-5472. CAN-06-2756
    • (2007) Cancer Res , vol.67 , pp. 5162-5171
    • Toyoshima, M.1    Tanaka, N.2    Aoki, J.3    Tanaka, Y.4    Murata, K.5    Kyuuma, M.6    Kobayashi, H.7    Ishii, N.8    Yaegashi, N.9    Sugamura, K.10
  • 222
    • 33644916118 scopus 로고    scopus 로고
    • Neuron to glia signaling triggers myelin membrane exocytosis from endosomal storage sites
    • 10.1083/jcb.200509022 1:CAS:528:DC%2BD28XisFKisLg%3D 16520383
    • Trajkovic K, Dhaunchak AS, Goncalves JT, Wenzel D, Schneider A, Bunt G, Nave KA, Simons M (2006) Neuron to glia signaling triggers myelin membrane exocytosis from endosomal storage sites. J Cell Biol 172:937-948. doi: 10.1083/jcb.200509022
    • (2006) J Cell Biol , vol.172 , pp. 937-948
    • Trajkovic, K.1    Dhaunchak, A.S.2    Goncalves, J.T.3    Wenzel, D.4    Schneider, A.5    Bunt, G.6    Nave, K.A.7    Simons, M.8
  • 224
    • 43249110449 scopus 로고    scopus 로고
    • Efficient and specific rescue of human immunodeficiency virus type 1 budding defects by a Nedd4-like ubiquitin ligase
    • 10.1128/JVI.02675-07 1:CAS:528:DC%2BD1cXlvVKisLY%3D 18321969
    • Usami Y, Popov S, Popova E, Göttlinger HG (2008) Efficient and specific rescue of human immunodeficiency virus type 1 budding defects by a Nedd4-like ubiquitin ligase. J Virol 82:4898-4907. doi: 10.1128/JVI.02675-07
    • (2008) J Virol , vol.82 , pp. 4898-4907
    • Usami, Y.1    Popov, S.2    Popova, E.3    Göttlinger, H.G.4
  • 226
    • 0026090892 scopus 로고
    • New SNF genes, GAL11 and GRR1 affect SUC2 expression in Saccharomyces cerevisiae
    • 1:CAS:528:DyaK38XhtVanu7o%3D 1752413
    • Vallier LG, Carlson M (1991) New SNF genes, GAL11 and GRR1 affect SUC2 expression in Saccharomyces cerevisiae. Genetics 129:675-684
    • (1991) Genetics , vol.129 , pp. 675-684
    • Vallier, L.G.1    Carlson, M.2
  • 227
    • 0035425122 scopus 로고    scopus 로고
    • A genomic view of yeast membrane transporters
    • 11454442
    • Van Belle D, André B (2001) A genomic view of yeast membrane transporters. Curr Opin Cell Biol 13:389-398
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 389-398
    • Van Belle, D.1    André, B.2
  • 229
    • 0345381737 scopus 로고    scopus 로고
    • The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor i receptor
    • 1:CAS:528:DC%2BD3sXjt1Glsbg%3D 12697834
    • Vecchione A, Marchese A, Henry P, Rotin D, Morrione A (2003) The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor. Mol Cell Biol 23:3363-3372
    • (2003) Mol Cell Biol , vol.23 , pp. 3363-3372
    • Vecchione, A.1    Marchese, A.2    Henry, P.3    Rotin, D.4    Morrione, A.5
  • 231
    • 0037240484 scopus 로고    scopus 로고
    • Visualization of TGN to endosome trafficking through fluorescently labeled MPR and AP-1 in living cells
    • 10.1091/mbc.E02-06-0338 1:CAS:528:DC%2BD3sXnvVOjtg%3D%3D 12529433
    • Waguri S, Dewitte F, Le Borgne R, Rouillé Y, Uchiyama Y, Dubremetz JF, Hoflack B (2003) Visualization of TGN to endosome trafficking through fluorescently labeled MPR and AP-1 in living cells. Mol Biol Cell 14:142-155. doi: 10.1091/mbc.E02-06-0338
    • (2003) Mol Biol Cell , vol.14 , pp. 142-155
    • Waguri, S.1    Dewitte, F.2    Le Borgne, R.3    Rouillé, Y.4    Uchiyama, Y.5    Dubremetz, J.F.6    Hoflack, B.7
  • 233
    • 79551653860 scopus 로고    scopus 로고
    • EXPO, an exocyst-positive organelle distinct from multivesicular endosomes and autophagosomes, mediates cytosol to cell wall exocytosis in Arabidopsis and tobacco cells
    • 10.1105/tpc.110.080697 1:CAS:528:DC%2BC3MXhvFGrt7w%3D 21193573
    • Wang J, Ding Y, Hillmer S, Miao Y, Lo SW, Wang X, Robinson DG, Jiang L (2010) EXPO, an exocyst-positive organelle distinct from multivesicular endosomes and autophagosomes, mediates cytosol to cell wall exocytosis in Arabidopsis and tobacco cells. Plant Cell 22:4009-4030. doi: 10.1105/tpc.110.080697
    • (2010) Plant Cell , vol.22 , pp. 4009-4030
    • Wang, J.1    Ding, Y.2    Hillmer, S.3    Miao, Y.4    Lo, S.W.5    Wang, X.6    Robinson, D.G.7    Jiang, L.8
  • 234
    • 84872089353 scopus 로고    scopus 로고
    • An update on channelopathies: From mechanisms to management
    • 10.1161/CIRCULATIONAHA.111.060343 23283857
    • Webster G, Berul CI (2013) An update on channelopathies: from mechanisms to management. Circulation 127:126-140. doi: 10.1161/CIRCULATIONAHA.111.060343
    • (2013) Circulation , vol.127 , pp. 126-140
    • Webster, G.1    Berul, C.I.2
  • 235
    • 33644872913 scopus 로고    scopus 로고
    • Exploring the ESCRTing machinery in eukaryotes
    • 10.1016/j.tplants.2006.01.008 1:CAS:528:DC%2BD28XisFyjsrw%3D 16488176
    • Winter V, Hauser MT (2006) Exploring the ESCRTing machinery in eukaryotes. Trends Plant Sci 11:115-123. doi: 10.1016/j.tplants.2006.01.008
    • (2006) Trends Plant Sci , vol.11 , pp. 115-123
    • Winter, V.1    Hauser, M.T.2
  • 237
    • 33745232336 scopus 로고    scopus 로고
    • Channeling studies in yeast: Yeast as a model for channelopathies?
    • 10.1385/NMM:8:3:279 1:CAS:528:DC%2BD28Xls1Shs7g%3D 16775381
    • Wolfe DM, Pearce DA (2006) Channeling studies in yeast: yeast as a model for channelopathies? Neuromolecular Med 8:279-306. doi: 10.1385/NMM:8:3:279
    • (2006) Neuromolecular Med , vol.8 , pp. 279-306
    • Wolfe, D.M.1    Pearce, D.A.2
  • 238
    • 62249210955 scopus 로고    scopus 로고
    • Membrane scission by the ESCRT-III complex
    • 10.1038/nature07836 1:CAS:528:DC%2BD1MXitFKltrk%3D 19234443
    • Wollert T, Wunder C, Lippincott-Schwartz J, Hurley JH (2009) Membrane scission by the ESCRT-III complex. Nature 458:172-177. doi: 10.1038/nature07836
    • (2009) Nature , vol.458 , pp. 172-177
    • Wollert, T.1    Wunder, C.2    Lippincott-Schwartz, J.3    Hurley, J.H.4
  • 239
    • 59749089436 scopus 로고    scopus 로고
    • ESCRT proteins, endosome organization and mitogenic receptor down-regulation
    • 10.1042/BST0370146 1:CAS:528:DC%2BD1MXotVWntw%3D%3D 19143620
    • Woodman P (2009) ESCRT proteins, endosome organization and mitogenic receptor down-regulation. Biochem Soc Trans 37:146-150. doi: 10.1042/BST0370146
    • (2009) Biochem Soc Trans , vol.37 , pp. 146-150
    • Woodman, P.1
  • 240
    • 79955940965 scopus 로고    scopus 로고
    • Regulation of endocytic sorting by ESCRT-DUB-mediated deubiquitination
    • 10.1007/s12013-011-9181-9 1:CAS:528:DC%2BC3MXmtVGhsrc%3D 21448666
    • Wright MH, Berlin I, Nash PD (2011) Regulation of endocytic sorting by ESCRT-DUB-mediated deubiquitination. Cell Biochem Biophys 60:39-46. doi: 10.1007/s12013-011-9181-9
    • (2011) Cell Biochem Biophys , vol.60 , pp. 39-46
    • Wright, M.H.1    Berlin, I.2    Nash, P.D.3
  • 244
    • 77449124047 scopus 로고    scopus 로고
    • Nedd4 and Nedd4-2: Closely related ubiquitin-protein ligases with distinct physiological functions
    • 10.1038/cdd.2009.84 1:CAS:528:DC%2BD1MXhsFGnurvJ 19557014
    • Yang B, Kumar S (2010) Nedd4 and Nedd4-2: closely related ubiquitin-protein ligases with distinct physiological functions. Cell Death Differ 17:68-77. doi: 10.1038/cdd.2009.84
    • (2010) Cell Death Differ , vol.17 , pp. 68-77
    • Yang, B.1    Kumar, S.2
  • 245
    • 3442900814 scopus 로고    scopus 로고
    • Molecular characterization of NbCHMP1 encoding a homolog of human CHMP1 in Nicotiana benthamiana
    • 1:CAS:528:DC%2BD2cXks1Cmtr4%3D 15179039
    • Yang KS, Jin UH, Kim J, Song K, Kim SJ, Hwang I, Lim YP, Pai HS (2004) Molecular characterization of NbCHMP1 encoding a homolog of human CHMP1 in Nicotiana benthamiana. Mol Cells 17:255-261
    • (2004) Mol Cells , vol.17 , pp. 255-261
    • Yang, K.S.1    Jin, U.H.2    Kim, J.3    Song, K.4    Kim, S.J.5    Hwang, I.6    Lim, Y.P.7    Pai, H.S.8
  • 246
    • 56349153585 scopus 로고    scopus 로고
    • Nedd4 augments the adaptive immune response by promoting ubiquitin-mediated degradation of Cbl-b in activated T cells
    • 10.1038/ni.1670 1:CAS:528:DC%2BD1cXhtlOjsb3N 18931680
    • Yang B, Gay DL, MacLeod MK, Cao X, Hala T, Sweezer EM, Kappler J, Marrack P, Oliver PM (2008) Nedd4 augments the adaptive immune response by promoting ubiquitin-mediated degradation of Cbl-b in activated T cells. Nat Immunol 9:1356-1363. doi: 10.1038/ni.1670
    • (2008) Nat Immunol , vol.9 , pp. 1356-1363
    • Yang, B.1    Gay, D.L.2    Macleod, M.K.3    Cao, X.4    Hala, T.5    Sweezer, E.M.6    Kappler, J.7    Marrack, P.8    Oliver, P.M.9
  • 247
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • 10.1038/nrm2780 1:CAS:528:DC%2BD1MXhtlSjtbfM 19851334
    • Ye Y, Rape M (2009) Building ubiquitin chains: E2 enzymes at work. Nat Rev Mol Cell Biol 10:755-764. doi: 10.1038/nrm2780
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 248
    • 17144364368 scopus 로고    scopus 로고
    • + exchangers in the change of petal color during flower opening of Morning Glory, Ipomoea tricolor cv. Heavenly Blue
    • 10.1093/pcp/pci057 1:CAS:528:DC%2BD2MXjtVyisrs%3D 15695444
    • + exchangers in the change of petal color during flower opening of Morning Glory, Ipomoea tricolor cv. Heavenly Blue. Plant Cell Physiol 46:407-415. doi: 10.1093/pcp/pci057
    • (2005) Plant Cell Physiol , vol.46 , pp. 407-415
    • Yoshida, K.1    Kawachi, M.2    Mori, M.3    Maeshima, M.4    Kondo, M.5    Nishimura, M.6    Kondo, T.7
  • 249
    • 1642576972 scopus 로고    scopus 로고
    • + channel inhibitor identified by high-throughput screening in yeast
    • 10.1124/mol.65.1.214 1:CAS:528:DC%2BD2cXivVChs7s%3D 14722253
    • + channel inhibitor identified by high-throughput screening in yeast. Mol Pharmacol 65:214-219. doi: 10.1124/mol.65.1.214
    • (2004) Mol Pharmacol , vol.65 , pp. 214-219
    • Zaks-Makhina, E.1    Kim, Y.2    Aizenman, E.3    Levitan, E.S.4
  • 251
    • 77954583000 scopus 로고    scopus 로고
    • Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a Pseudomonas syringae effector
    • 10.1016/j.chom.2010.03.007 1:CAS:528:DC%2BC3cXlsVWqsrk%3D 20413097
    • Zhang J, Li W, Xiang T, Liu Z, Laluk K, Ding X, Zou Y, Gao M, Zhang X, Chen S, Mengiste T, Zhang Y, Zhou JM (2010) Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a Pseudomonas syringae effector. Cell Host Microbe 7:290-301. doi: 10.1016/j.chom.2010.03.007
    • (2010) Cell Host Microbe , vol.7 , pp. 290-301
    • Zhang, J.1    Li, W.2    Xiang, T.3    Liu, Z.4    Laluk, K.5    Ding, X.6    Zou, Y.7    Gao, M.8    Zhang, X.9    Chen, S.10    Mengiste, T.11    Zhang, Y.12    Zhou, J.M.13
  • 252
    • 84878389427 scopus 로고    scopus 로고
    • Knockout of the VPS22 component of the ESCRT-II complex in rice (Oryza sativa L.) causes chalky endosperm and early seedling lethality
    • 10.1007/s11033-012-2422-1 1:CAS:528:DC%2BC3sXkslagtLo%3D 23275199
    • Zhang XQ, Hou P, Zhu HT, Li GD, Liu XG, Xie XM (2013) Knockout of the VPS22 component of the ESCRT-II complex in rice (Oryza sativa L.) causes chalky endosperm and early seedling lethality. Mol Biol Rep 40:3475-3481. doi: 10.1007/s11033-012-2422-1
    • (2013) Mol Biol Rep , vol.40 , pp. 3475-3481
    • Zhang, X.Q.1    Hou, P.2    Zhu, H.T.3    Li, G.D.4    Liu, X.G.5    Xie, X.M.6
  • 253
    • 77957266397 scopus 로고    scopus 로고
    • + channel between endosomal degradation and recycling pathways
    • 10.1074/jbc.M110.150755 1:CAS:528:DC%2BC3cXht1Slsr3F 20675381
    • + channel between endosomal degradation and recycling pathways. J Biol Chem 285:30523-30530. doi: 10.1074/jbc.M110. 150755
    • (2010) J Biol Chem , vol.285 , pp. 30523-30530
    • Zhou, R.1    Kabra, R.2    Olson, D.R.3    Piper, R.C.4    Snyder, P.M.5
  • 254
    • 1842374437 scopus 로고    scopus 로고
    • MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/ cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5
    • 1:CAS:528:DyaK2sXmsVaktrc%3D 9055070
    • Zoladek T, Tobiasz A, Vaduva G, Boguta M, Martin NC, Hopper AK (1997) MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5. Genetics 145:595-603
    • (1997) Genetics , vol.145 , pp. 595-603
    • Zoladek, T.1    Tobiasz, A.2    Vaduva, G.3    Boguta, M.4    Martin, N.C.5    Hopper, A.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.