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Volumn 13, Issue 11, 2014, Pages 2871-2882

Identification of candidate substrates for the golgi tul1 E3 ligase using quantitative diGly proteomics in yeast

Author keywords

[No Author keywords available]

Indexed keywords

ESCRT PROTEIN; FUNGAL ENZYME; GOLGI TUL1 E3 LIGASE; STEROL REGULATORY ELEMENT BINDING PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; DESMOCOLLIN; PEP12 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SYNTAXIN; TUL1 PROTEIN, S CEREVISIAE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBX3 PROTEIN, S CEREVISIAE;

EID: 84910673082     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.040774     Document Type: Article
Times cited : (29)

References (55)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W. E., Morimoto, R. I., Dillin, A., and Kelly, J. W. (2008) Adapting proteostasis for disease intervention. Science 319, 916-919
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 2
    • 84897129156 scopus 로고    scopus 로고
    • Differential scales of protein quality control
    • Wolff, S., Weissman, J. S., and Dillin, A. (2014) Differential scales of protein quality control. Cell 157, 52-64
    • (2014) Cell , vol.157 , pp. 52-64
    • Wolff, S.1    Weissman, J.S.2    Dillin, A.3
  • 3
    • 84867176120 scopus 로고    scopus 로고
    • The ubiquitinproteasome system of Saccharomyces cerevisiae
    • Finley, D., Ulrich, H. D., Sommer, T., and Kaiser, P. (2012) The ubiquitinproteasome system of Saccharomyces cerevisiae. Genetics 192, 319-360
    • (2012) Genetics , vol.192 , pp. 319-360
    • Finley, D.1    Ulrich, H.D.2    Sommer, T.3    Kaiser, P.4
  • 5
    • 84865298998 scopus 로고    scopus 로고
    • Finding the will and the way of ERAD substrate retrotranslocation
    • Hampton, R. Y., and Sommer, T. (2012) Finding the will and the way of ERAD substrate retrotranslocation. Curr. Opin. Cell Biol. 24, 460-466
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 460-466
    • Hampton, R.Y.1    Sommer, T.2
  • 6
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • Brodsky, J. L. (2012) Cleaning up: ER-associated degradation to the rescue. Cell 151, 1163-1167
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 7
    • 77649296829 scopus 로고    scopus 로고
    • Sterol regulatory element binding proteins in fungi: Hypoxic transcription factors linked to pathogenesis
    • Bien, C. M., and Espenshade, P. J. (2010) Sterol regulatory element binding proteins in fungi: hypoxic transcription factors linked to pathogenesis. Eukaryot. Cell 9, 352-359
    • (2010) Eukaryot. Cell , vol.9 , pp. 352-359
    • Bien, C.M.1    Espenshade, P.J.2
  • 9
    • 84855288996 scopus 로고    scopus 로고
    • Yeast sterol regulatory element-binding protein (SREBP) cleavage requires Cdc48 and Dsc5, a ubiquitin regulatory X domain-containing subunit of the Golgi Dsc E3 ligase
    • Stewart, E. V., Lloyd, S. J., Burg, J. S., Nwosu, C. C., Lintner, R. E., Daza, R., Russ, C., Ponchner, K., Nusbaum, C., and Espenshade, P. J. (2012) Yeast sterol regulatory element-binding protein (SREBP) cleavage requires Cdc48 and Dsc5, a ubiquitin regulatory X domain-containing subunit of the Golgi Dsc E3 ligase. J. Biol. Chem. 287, 672-681
    • (2012) J. Biol. Chem. , vol.287 , pp. 672-681
    • Stewart, E.V.1    Lloyd, S.J.2    Burg, J.S.3    Nwosu, C.C.4    Lintner, R.E.5    Daza, R.6    Russ, C.7    Ponchner, K.8    Nusbaum, C.9    Espenshade, P.J.10
  • 10
    • 84880519236 scopus 로고    scopus 로고
    • Subunit architecture of the Golgi Dsc E3 ligase required for sterol regulatory element-binding protein (SREBP) cleavage in fission yeast
    • Lloyd, S. J., Raychaudhuri, S., and Espenshade, P. J. (2013) Subunit architecture of the Golgi Dsc E3 ligase required for sterol regulatory element-binding protein (SREBP) cleavage in fission yeast. J. Biol. Chem. 288, 21043-21054
    • (2013) J. Biol. Chem. , vol.288 , pp. 21043-21054
    • Lloyd, S.J.1    Raychaudhuri, S.2    Espenshade, P.J.3
  • 13
    • 0036166924 scopus 로고    scopus 로고
    • A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies
    • Reggiori, F., and Pelham, H. R. (2002) A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies. Nat. Cell Biol. 4, 117-123
    • (2002) Nat. Cell Biol. , vol.4 , pp. 117-123
    • Reggiori, F.1    Pelham, H.R.2
  • 14
    • 23044444831 scopus 로고    scopus 로고
    • Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation
    • Valdez-Taubas, J., and Pelham, H. (2005) Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation. EMBO J. 24, 2524-2532
    • (2005) EMBO J. , vol.24 , pp. 2524-2532
    • Valdez-Taubas, J.1    Pelham, H.2
  • 15
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann, M. (2006) Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 7, 952-958
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 952-958
    • Mann, M.1
  • 16
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 17
    • 40649095957 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture
    • Harsha, H. C., Molina, H., and Pandey, A. (2008) Quantitative proteomics using stable isotope labeling with amino acids in cell culture. Nat. Protoc. 3, 505-516
    • (2008) Nat. Protoc. , vol.3 , pp. 505-516
    • Harsha, H.C.1    Molina, H.2    Pandey, A.3
  • 18
    • 84890604300 scopus 로고    scopus 로고
    • Using the ubiquitin-modified proteome to monitor protein homeostasis function
    • Carrano, A. C., and Bennett, E. J. (2013) Using the ubiquitin-modified proteome to monitor protein homeostasis function. Mol. Cell. Proteomics 12, 3521-3531
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3521-3531
    • Carrano, A.C.1    Bennett, E.J.2
  • 19
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu, G., Paige, J. S., and Jaffrey, S. R. (2010) Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat. Biotechnol. 28, 868-873
    • (2010) Nat. Biotechnol. , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 24
    • 82355164206 scopus 로고    scopus 로고
    • Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels
    • Lee, K. A., Hammerle, L. P., Andrews, P. S., Stokes, M. P., Mustelin, T., Silva, J. C., Black, R. A., and Doedens, J. R. (2011) Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels. J. Biol. Chem. 286, 41530-41538
    • (2011) J. Biol. Chem. , vol.286 , pp. 41530-41538
    • Lee, K.A.1    Hammerle, L.P.2    Andrews, P.S.3    Stokes, M.P.4    Mustelin, T.5    Silva, J.C.6    Black, R.A.7    Doedens, J.R.8
  • 28
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in saccharomyces cerevisiae
    • Longtine, M. S., McKenzie, A., 3rd, Demarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P., and Pringle, J. R. (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.S.1    McKenzie, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 29
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, J., Hochstrasser, M., Finley, D., and Peng, J. (2009) Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137, 133-145
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5    Robert, J.6    Rush, J.7    Hochstrasser, M.8    Finley, D.9    Peng, J.10
  • 31
    • 17644401005 scopus 로고    scopus 로고
    • SREBP pathway responds to sterols and functions as an oxygen sensor in fission yeast
    • Hughes, A. L., Todd, B. L., and Espenshade, P. J. (2005) SREBP pathway responds to sterols and functions as an oxygen sensor in fission yeast. Cell 120, 831-842
    • (2005) Cell , vol.120 , pp. 831-842
    • Hughes, A.L.1    Todd, B.L.2    Espenshade, P.J.3
  • 32
    • 34548454995 scopus 로고    scopus 로고
    • SREBP controls oxygen-dependent mobilization of retrotransposons in fission yeast
    • Sehgal, A., Lee, C. Y., and Espenshade, P. J. (2007) SREBP controls oxygen-dependent mobilization of retrotransposons in fission yeast. PLoS Genet. 3, 1389-1396
    • (2007) PLoS Genet. , vol.3 , pp. 1389-1396
    • Sehgal, A.1    Lee, C.Y.2    Espenshade, P.J.3
  • 34
    • 84864131300 scopus 로고    scopus 로고
    • Analysis of ubiquitinated proteome by quantitative mass spectrometry
    • Na, C. H., and Peng, J. (2012) Analysis of ubiquitinated proteome by quantitative mass spectrometry. Methods Mol. Biol. 893, 417-429
    • (2012) Methods Mol. Biol. , vol.893 , pp. 417-429
    • Na, C.H.1    Peng, J.2
  • 35
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V., and Mann, M. (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 36
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micropurification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber, J., Mann, M., and Ishihama, Y. (2007) Protocol for micropurification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2, 1896-1906
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 37
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 41
    • 84872840929 scopus 로고    scopus 로고
    • Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover
    • Olzmann, J. A., Richter, C. M., and Kopito, R. R. (2013) Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover. Proc. Natl. Acad. Sci. U.S.A. 110, 1345-1350
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 1345-1350
    • Olzmann, J.A.1    Richter, C.M.2    Kopito, R.R.3
  • 42
    • 80455164551 scopus 로고    scopus 로고
    • Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant alpha-1 antitrypsin from the endoplasmic reticulum
    • Greenblatt, E. J., Olzmann, J. A., and Kopito, R. R. (2011) Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant alpha-1 antitrypsin from the endoplasmic reticulum. Nat. Struct. Mol. Biol. 18, 1147-1152
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1147-1152
    • Greenblatt, E.J.1    Olzmann, J.A.2    Kopito, R.R.3
  • 43
    • 84876806705 scopus 로고    scopus 로고
    • Sampling the membrane: Function of rhomboidfamily proteins
    • Lemberg, M. K. (2013) Sampling the membrane: function of rhomboidfamily proteins. Trends Cell Biol. 23, 210-217
    • (2013) Trends Cell Biol. , vol.23 , pp. 210-217
    • Lemberg, M.K.1
  • 44
    • 52649138958 scopus 로고    scopus 로고
    • UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover
    • Alexandru, G., Graumann, J., Smith, G. T., Kolawa, N. J., Fang, R., and Deshaies, R. J. (2008) UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 134, 804-816
    • (2008) Cell , vol.134 , pp. 804-816
    • Alexandru, G.1    Graumann, J.2    Smith, G.T.3    Kolawa, N.J.4    Fang, R.5    Deshaies, R.J.6
  • 46
    • 0034735540 scopus 로고    scopus 로고
    • A selective transport route from Golgi to late endosomes that requires the yeast GGA proteins
    • Black, M. W., and Pelham, H. R. (2000) A selective transport route from Golgi to late endosomes that requires the yeast GGA proteins. J. Cell Biol. 151, 587-600
    • (2000) J. Cell Biol. , vol.151 , pp. 587-600
    • Black, M.W.1    Pelham, H.R.2
  • 47
    • 0030012162 scopus 로고    scopus 로고
    • Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast
    • Becherer, K. A., Rieder, S. E., Emr, S. D., and Jones, E. W. (1996) Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast. Mol. Biol. Cell 7, 579-594
    • (1996) Mol. Biol. Cell , vol.7 , pp. 579-594
    • Becherer, K.A.1    Rieder, S.E.2    Emr, S.D.3    Jones, E.W.4
  • 48
    • 0033739781 scopus 로고    scopus 로고
    • Polar transmembrane domains target proteins to the interior of the yeast vacuole
    • Reggiori, F., Black, M. W., and Pelham, H. R. (2000) Polar transmembrane domains target proteins to the interior of the yeast vacuole. Mol. Biol. Cell 11, 3737-3749
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3737-3749
    • Reggiori, F.1    Black, M.W.2    Pelham, H.R.3
  • 50
    • 0032794445 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast
    • Swaminathan, S., Amerik, A. Y., and Hochstrasser, M. (1999) The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. Mol. Biol. Cell 10, 2583-2594
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2583-2594
    • Swaminathan, S.1    Amerik, A.Y.2    Hochstrasser, M.3
  • 51
    • 84868678524 scopus 로고    scopus 로고
    • The running of the Buls: Control of permease trafficking by alpha-arrestins Bul1 and Bul2
    • O'Donnell, A. F. (2012) The running of the Buls: control of permease trafficking by alpha-arrestins Bul1 and Bul2. Mol. Cell. Biol. 32, 4506-4509
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4506-4509
    • O'Donnell, A.F.1
  • 52
    • 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
    • Merhi, A., and Andre, 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
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4510-4522
    • Merhi, A.1    Andre, B.2
  • 53
    • 84867025125 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of endocytosis by proteins of the arrestin family
    • Becuwe, M., Herrador, A., Haguenauer-Tsapis, R., Vincent, O., and Leon, S. (2012) Ubiquitin-mediated regulation of endocytosis by proteins of the arrestin family. Biochem. Res. Int. 2012, 242764
    • (2012) Biochem. Res. Int. , vol.2012 , pp. 242764
    • Becuwe, M.1    Herrador, A.2    Haguenauer-Tsapis, R.3    Vincent, O.4    Leon, S.5
  • 54
    • 33845970909 scopus 로고    scopus 로고
    • The deubiquitinating enzyme Ubp2 modulates Rsp5-dependent Lys63-linked polyubiquitin conjugates in Saccharomyces cerevisiae
    • Kee, Y., Munoz, W., Lyon, N., and Huibregtse, J. M. (2006) The deubiquitinating enzyme Ubp2 modulates Rsp5-dependent Lys63-linked polyubiquitin conjugates in Saccharomyces cerevisiae. J. Biol. Chem. 281, 36724-36731
    • (2006) J. Biol. Chem. , vol.281 , pp. 36724-36731
    • Kee, Y.1    Munoz, W.2    Lyon, N.3    Huibregtse, J.M.4


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