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Volumn 7, Issue 6, 2012, Pages

Rsp5 Ubiquitin Ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutants

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CYTOSKELETON PROTEIN; MEMBRANE PROTEIN; NEOMYCIN; PROTEIN COPI; PROTEIN KAR2P; PROTEIN RER1P; PROTEIN RSP5; PROTEIN SEC27; PROTEIN SLA1; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84862735467     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0039582     Document Type: Article
Times cited : (20)

References (54)
  • 2
    • 0028643562 scopus 로고
    • Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum
    • Letourneur F, Gaynor E, Hennecke S, Démollière C, Duden R, et al. (1994) Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. Cell 79: 1199-1207.
    • (1994) Cell , vol.79 , pp. 1199-1207
    • Letourneur, F.1    Gaynor, E.2    Hennecke, S.3    Démollière, C.4    Duden, R.5
  • 3
    • 0001264854 scopus 로고    scopus 로고
    • The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation
    • Wu W, Erickson J, Lin R, Cerione R, (2000) The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 405: 800-804.
    • (2000) Nature , vol.405 , pp. 800-804
    • Wu, W.1    Erickson, J.2    Lin, R.3    Cerione, R.4
  • 4
    • 0035809932 scopus 로고    scopus 로고
    • Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer
    • Sato K, Sato M, Nakano A, (2001) Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer. J Cell Biol 152: 935-944.
    • (2001) J Cell Biol , vol.152 , pp. 935-944
    • Sato, K.1    Sato, M.2    Nakano, A.3
  • 5
    • 33846130922 scopus 로고    scopus 로고
    • Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast
    • Gabriely G, Kama R, Gerst J, (2007) Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast. Mol Cell Biol 27: 526-540.
    • (2007) Mol Cell Biol , vol.27 , pp. 526-540
    • Gabriely, G.1    Kama, R.2    Gerst, J.3
  • 6
    • 33745413038 scopus 로고    scopus 로고
    • The Gcs1 Arf-GAP mediates Snc1,2 v-SNARE retrieval to the Golgi in yeast
    • Robinson M, Poon P, Schindler C, Murray L, Kama R, et al. (2006) The Gcs1 Arf-GAP mediates Snc1,2 v-SNARE retrieval to the Golgi in yeast. Mol Biol Cell 17: 1845-1858.
    • (2006) Mol Biol Cell , vol.17 , pp. 1845-1858
    • Robinson, M.1    Poon, P.2    Schindler, C.3    Murray, L.4    Kama, R.5
  • 7
    • 0242300110 scopus 로고    scopus 로고
    • A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery
    • Hitchcock A, Auld K, Gygi S, Silver P, (2003) A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc Natl Acad Sci U S A 100: 12735-12740.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12735-12740
    • Hitchcock, A.1    Auld, K.2    Gygi, S.3    Silver, P.4
  • 8
    • 0041706156 scopus 로고    scopus 로고
    • A proteomics approach to understanding protein ubiquitination
    • Peng J, Schwartz D, Elias J, Thoreen C, Cheng D, et al. (2003) A proteomics approach to understanding protein ubiquitination. Nat Biotechnol 21: 921-926.
    • (2003) Nat Biotechnol , vol.21 , pp. 921-926
    • Peng, J.1    Schwartz, D.2    Elias, J.3    Thoreen, C.4    Cheng, D.5
  • 9
    • 1542373897 scopus 로고    scopus 로고
    • Distinct monoubiquitin signals in receptor endocytosis
    • Haglund K, Di Fiore P, Dikic I, (2003) Distinct monoubiquitin signals in receptor endocytosis. Trends Biochem Sci 28: 598-603.
    • (2003) Trends Biochem Sci , vol.28 , pp. 598-603
    • Haglund, K.1    Di Fiore, P.2    Dikic, I.3
  • 10
    • 0038362292 scopus 로고    scopus 로고
    • When ubiquitin meets ubiquitin receptors: a signalling connection
    • Di Fiore P, Polo S, Hofmann K, (2003) When ubiquitin meets ubiquitin receptors: a signalling connection. Nat Rev Mol Cell Biol 4: 491-497.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 491-497
    • Di Fiore, P.1    Polo, S.2    Hofmann, K.3
  • 11
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • Mukhopadhyay D, Riezman H, (2007) Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 315: 201-205.
    • (2007) Science , vol.315 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 13
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series
    • Ikeda F, Dikic I, (2008) Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series. EMBO Rep 9: 536-542.
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 14
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M, (1996) Ubiquitin-dependent protein degradation. Annu Rev Genet 30: 405-439.
    • (1996) Annu Rev Genet , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 15
    • 67649227630 scopus 로고    scopus 로고
    • Polyubiquitination by HECT E3s and the determinants of chain type specificity
    • Kim HC, Huibregtse JM, (2009) Polyubiquitination by HECT E3s and the determinants of chain type specificity. Mol Cell Biol 29: 3307-3318.
    • (2009) Mol Cell Biol , vol.29 , pp. 3307-3318
    • Kim, H.C.1    Huibregtse, J.M.2
  • 19
    • 22744456248 scopus 로고    scopus 로고
    • The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme
    • Kee Y, Lyon N, Huibregtse J, (2005) The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme. EMBO J 24: 2414-2424.
    • (2005) EMBO J , vol.24 , pp. 2414-2424
    • Kee, Y.1    Lyon, N.2    Huibregtse, J.3
  • 20
    • 50249128591 scopus 로고    scopus 로고
    • Is the Rsp5 ubiquitin ligase involved in the regulation of ribophagy?
    • Kraft C, Peter M, (2008) Is the Rsp5 ubiquitin ligase involved in the regulation of ribophagy? Autophagy 4: 838-840.
    • (2008) Autophagy , vol.4 , pp. 838-840
    • Kraft, C.1    Peter, M.2
  • 21
    • 78149408945 scopus 로고    scopus 로고
    • The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23
    • Ossareh-Nazari B, Cohen M, Dargemont C, (2010) The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23. Exp Cell Res 316: 3351-3357.
    • (2010) Exp Cell Res , vol.316 , pp. 3351-3357
    • Ossareh-Nazari, B.1    Cohen, M.2    Dargemont, C.3
  • 22
    • 0346101801 scopus 로고    scopus 로고
    • Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport
    • Cohen M, Stutz F, Dargemont C, (2003) Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport. J Biol Chem 278: 51989-51992.
    • (2003) J Biol Chem , vol.278 , pp. 51989-51992
    • Cohen, M.1    Stutz, F.2    Dargemont, C.3
  • 23
    • 34147217542 scopus 로고    scopus 로고
    • Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map
    • Collins SR, Miller KM, Maas NL, Roguev A, Fillingham J, et al. (2007) Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. Nature 446: 806-810.
    • (2007) Nature , vol.446 , pp. 806-810
    • Collins, S.R.1    Miller, K.M.2    Maas, N.L.3    Roguev, A.4    Fillingham, J.5
  • 24
    • 0035155749 scopus 로고    scopus 로고
    • WW domains of Rsp5p define different functions: determination of roles in fluid phase and uracil permease endocytosis in Saccharomyces cerevisiae
    • Gajewska B, Kamińska J, Jesionowska A, Martin N, Hopper A, et al. (2001) WW domains of Rsp5p define different functions: determination of roles in fluid phase and uracil permease endocytosis in Saccharomyces cerevisiae. Genetics 157: 91-101.
    • (2001) Genetics , vol.157 , pp. 91-101
    • Gajewska, B.1    Kamińska, J.2    Jesionowska, A.3    Martin, N.4    Hopper, A.5
  • 25
    • 33645576669 scopus 로고    scopus 로고
    • Enhanced levels of Pis1p (phosphatidylinositol synthase) improve the growth of Saccharomyces cerevisiae cells deficient in Rsp5 ubiquitin ligase
    • Kaliszewski P, Ferreira T, Gajewska B, Szkopinska A, Berges T, et al. (2006) Enhanced levels of Pis1p (phosphatidylinositol synthase) improve the growth of Saccharomyces cerevisiae cells deficient in Rsp5 ubiquitin ligase. Biochem J 395: 173-181.
    • (2006) Biochem J , vol.395 , pp. 173-181
    • Kaliszewski, P.1    Ferreira, T.2    Gajewska, B.3    Szkopinska, A.4    Berges, T.5
  • 26
    • 26844489762 scopus 로고    scopus 로고
    • Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile
    • Schuldiner M, Collins SR, Thompson NJ, Denic V, Bhamidipati A, et al. (2005) Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123: 507-519.
    • (2005) Cell , vol.123 , pp. 507-519
    • Schuldiner, M.1    Collins, S.R.2    Thompson, N.J.3    Denic, V.4    Bhamidipati, A.5
  • 28
    • 34547843498 scopus 로고    scopus 로고
    • Targeting of Sna3p to the endosomal pathway depends on its interaction with Rsp5p and multivesicular body sorting on its ubiquitylation
    • Stawiecka-Mirota M, Pokrzywa W, Morvan J, Zoladek T, Haguenauer-Tsapis R, et al. (2007) Targeting of Sna3p to the endosomal pathway depends on its interaction with Rsp5p and multivesicular body sorting on its ubiquitylation. Traffic 8: 1280-1296.
    • (2007) Traffic , vol.8 , pp. 1280-1296
    • Stawiecka-Mirota, M.1    Pokrzywa, W.2    Morvan, J.3    Zoladek, T.4    Haguenauer-Tsapis, R.5
  • 29
    • 0030868677 scopus 로고    scopus 로고
    • Interaction of coatomer with aminoglycoside antibiotics: evidence that coatomer has at least two dilysine binding sites
    • Hudson R, Draper R, (1997) Interaction of coatomer with aminoglycoside antibiotics: evidence that coatomer has at least two dilysine binding sites. Mol Biol Cell 8: 1901-1910.
    • (1997) Mol Biol Cell , vol.8 , pp. 1901-1910
    • Hudson, R.1    Draper, R.2
  • 30
    • 7544228190 scopus 로고    scopus 로고
    • The HECT E3 ubiquitin ligase Rsp5 is important for ubiquitin homeostasis in yeast
    • Krsmanović T, Kölling R, (2004) The HECT E3 ubiquitin ligase Rsp5 is important for ubiquitin homeostasis in yeast. FEBS Lett 577: 215-219.
    • (2004) FEBS Lett , vol.577 , pp. 215-219
    • Krsmanović, T.1    Kölling, R.2
  • 31
    • 0035903635 scopus 로고    scopus 로고
    • Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting
    • Reggiori F, Pelham HR, (2001) Sorting of proteins into multivesicular bodies: ubiquitin-dependent and-independent targeting. EMBO J 20: 5176-5186.
    • (2001) EMBO J , vol.20 , pp. 5176-5186
    • Reggiori, F.1    Pelham, H.R.2
  • 32
    • 0036786951 scopus 로고    scopus 로고
    • Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae
    • Kamińska J, Gajewska B, Hopper A, Zoladek T, (2002) Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae. Mol Cell Biol 22: 6946-6948.
    • (2002) Mol Cell Biol , vol.22 , pp. 6946-6948
    • Kamińska, J.1    Gajewska, B.2    Hopper, A.3    Zoladek, T.4
  • 33
    • 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
    • Zoladek T, Tobiasz A, Vaduva G, Boguta M, Martin N, et al. (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.5
  • 34
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst M, Sato T, Banta L, Emr S, (1997) Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J 16: 1820-1831.
    • (1997) EMBO J , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.2    Banta, L.3    Emr, S.4
  • 35
    • 0742288063 scopus 로고    scopus 로고
    • Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S
    • Katzmann DJ, Sarkar S, Chu T, Audhya A, Emr SD, (2004) Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S. Mol Biol Cell 15: 468-480.
    • (2004) Mol Biol Cell , vol.15 , pp. 468-480
    • Katzmann, D.J.1    Sarkar, S.2    Chu, T.3    Audhya, A.4    Emr, S.D.5
  • 36
    • 0030665269 scopus 로고    scopus 로고
    • Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast
    • Sütterlin C, Doering T, Schimmöller F, Schröder S, Riezman H, (1997) Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast. J Cell Sci 110 (Pt 21): 2703-2714.
    • (1997) J Cell Sci , vol.110 , Issue.Pt 21 , pp. 2703-2714
    • Sütterlin, C.1    Doering, T.2    Schimmöller, F.3    Schröder, S.4    Riezman, H.5
  • 37
    • 1942439642 scopus 로고    scopus 로고
    • Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins
    • Hettema E, Valdez-Taubas J, Pelham H, (2004) Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins. EMBO J 23: 1279-1288.
    • (2004) EMBO J , vol.23 , pp. 1279-1288
    • Hettema, E.1    Valdez-Taubas, J.2    Pelham, H.3
  • 38
    • 1542344041 scopus 로고    scopus 로고
    • The alpha- and beta'-COP WD40 domains mediate cargo-selective interactions with distinct di-lysine motifs
    • Eugster A, Frigerio G, Dale M, Duden R, (2004) The alpha- and beta'-COP WD40 domains mediate cargo-selective interactions with distinct di-lysine motifs. Mol Biol Cell 15: 1011-1023.
    • (2004) Mol Biol Cell , vol.15 , pp. 1011-1023
    • Eugster, A.1    Frigerio, G.2    Dale, M.3    Duden, R.4
  • 39
    • 0028031043 scopus 로고
    • Retrieval of HDEL proteins is required for growth of yeast cells
    • Townsley FM, Frigerio G, Pelham HR, (1994) Retrieval of HDEL proteins is required for growth of yeast cells. J Cell Biol 127: 21-28.
    • (1994) J Cell Biol , vol.127 , pp. 21-28
    • Townsley, F.M.1    Frigerio, G.2    Pelham, H.R.3
  • 40
    • 73949101221 scopus 로고    scopus 로고
    • Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation
    • Harreman M, Taschner M, Sigurdsson S, Anindya R, Reid J, et al. (2009) Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proc Natl Acad Sci U S A 106: 20705-20710.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 20705-20710
    • Harreman, M.1    Taschner, M.2    Sigurdsson, S.3    Anindya, R.4    Reid, J.5
  • 41
    • 78149456945 scopus 로고    scopus 로고
    • WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins
    • Pashkova N, Gakhar L, Winistorfer SC, Yu L, Ramaswamy S, et al. (2010) WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins. Mol Cell 40: 433-443.
    • (2010) Mol Cell , vol.40 , pp. 433-443
    • Pashkova, N.1    Gakhar, L.2    Winistorfer, S.C.3    Yu, L.4    Ramaswamy, S.5
  • 42
    • 1942437556 scopus 로고    scopus 로고
    • The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167
    • Stamenova S, Dunn R, Adler A, Hicke L, (2004) The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167. J Biol Chem 279: 16017-16025.
    • (2004) J Biol Chem , vol.279 , pp. 16017-16025
    • Stamenova, S.1    Dunn, R.2    Adler, A.3    Hicke, L.4
  • 43
    • 0034734849 scopus 로고    scopus 로고
    • A network of proteins around Rvs167p and Rvs161p, two proteins related to the yeast actin cytoskeleton
    • Bon E, Recordon-Navarro P, Durrens P, Iwase M, Toh-E A, et al. (2000) A network of proteins around Rvs167p and Rvs161p, two proteins related to the yeast actin cytoskeleton. Yeast 16: 1229-1241.
    • (2000) Yeast , vol.16 , pp. 1229-1241
    • Bon, E.1    Recordon-Navarro, P.2    Durrens, P.3    Iwase, M.4    Toh-E, A.5
  • 44
    • 0030932017 scopus 로고    scopus 로고
    • Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins
    • Sato K, Sato M, Nakano A, (1997) Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins. Proc Natl Acad Sci U S A 94: 9693-9698.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 9693-9698
    • Sato, K.1    Sato, M.2    Nakano, A.3
  • 45
    • 2442717708 scopus 로고    scopus 로고
    • The ubiquitin ligase Rsp5p is required for modification and sorting of membrane proteins into multivesicular bodies
    • Morvan J, Froissard M, Haguenauer-Tsapis R, Urban-Grimal D, (2004) The ubiquitin ligase Rsp5p is required for modification and sorting of membrane proteins into multivesicular bodies. Traffic 5: 383-392.
    • (2004) Traffic , vol.5 , pp. 383-392
    • Morvan, J.1    Froissard, M.2    Haguenauer-Tsapis, R.3    Urban-Grimal, D.4
  • 46
    • 0033048856 scopus 로고    scopus 로고
    • NH4+-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains
    • Springael JY, Galan JM, Haguenauer-Tsapis R, André B, (1999) NH4+-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains. J Cell Sci 112 (Pt 9): 1375-1383.
    • (1999) J Cell Sci , vol.112 , Issue.Pt 9 , pp. 1375-1383
    • Springael, J.Y.1    Galan, J.M.2    Haguenauer-Tsapis, R.3    André, B.4
  • 47
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • Sherman F, (2002) Getting started with yeast. Methods Enzymol 350: 3-41.
    • (2002) Methods Enzymol , vol.350 , pp. 3-41
    • Sherman, F.1
  • 48
    • 0026599048 scopus 로고
    • One-step transformation of yeast in stationary phase
    • Chen D, Yang B, Kuo T, (1992) One-step transformation of yeast in stationary phase. Curr Genet 21: 83-84.
    • (1992) Curr Genet , vol.21 , pp. 83-84
    • Chen, D.1    Yang, B.2    Kuo, T.3
  • 49
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine M, McKenzie Ar, Demarini D, Shah N, Wach A, et al. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14: 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.1    McKenzie, A.R.2    Demarini, D.3    Shah, N.4    Wach, A.5
  • 50
    • 0035159694 scopus 로고    scopus 로고
    • Deletion of yeast p24 genes activates the unfolded protein response
    • Belden W, Barlowe C, (2001) Deletion of yeast p24 genes activates the unfolded protein response. Mol Biol Cell 12: 957-969.
    • (2001) Mol Biol Cell , vol.12 , pp. 957-969
    • Belden, W.1    Barlowe, C.2
  • 51
    • 0024342479 scopus 로고
    • Characterization of the END1 gene required for vacuole biogenesis and gluconeogenic growth of budding yeast
    • Dulić V, Riezman H, (1989) Characterization of the END1 gene required for vacuole biogenesis and gluconeogenic growth of budding yeast. EMBO J 8: 1349-1359.
    • (1989) EMBO J , vol.8 , pp. 1349-1359
    • Dulić, V.1    Riezman, H.2
  • 52
    • 0024518932 scopus 로고
    • The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex
    • Bankaitis VA, Malehorn DE, Emr SD, Greene R, (1989) The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex. J Cell Biol 108: 1271-1281.
    • (1989) J Cell Biol , vol.108 , pp. 1271-1281
    • Bankaitis, V.A.1    Malehorn, D.E.2    Emr, S.D.3    Greene, R.4
  • 53
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor
    • Chen P, Johnson P, Sommer T, Jentsch S, Hochstrasser M, (1993) Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor. Cell 74: 357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 54
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa F, Hochstrasser M, (1993) The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 366: 313-319.
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.1    Hochstrasser, M.2


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