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Volumn 12, Issue 10, 2013, Pages 2791-2803

Perturbations to the ubiquitin conjugate proteome in yeast aubx mutants identify Ubx2 as a regulator of membrane lipid composition

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A DESATURASE; ADENOSINE TRIPHOSPHATASE; CDC48 PROTEIN; FUNGAL PROTEIN; MEMBRANE LIPID; MEMBRANE PROTEIN; PROTEIN P90; PROTEOME; REGULATOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR SPT23; UBIQUITIN CONJUGATE PROTEOME; UBIQUITINATED PROTEIN; UBX2 PROTEIN; UNCLASSIFIED DRUG;

EID: 84885112498     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M113.030163     Document Type: Article
Times cited : (24)

References (58)
  • 3
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer, H., Bug, M., and Bremer, S. (2012) Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat. Cell Biol. 14, 117-123
    • (2012) Nat. Cell Biol. , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 4
    • 33749236210 scopus 로고    scopus 로고
    • Diverse functions with a common regulator: Ubiquitin takes command of an AAA ATPase
    • Ye, Y. (2006) Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase. J. Struct. Biol. 156, 29-40
    • (2006) J. Struct. Biol. , vol.156 , pp. 29-40
    • Ye, Y.1
  • 7
    • 79951625225 scopus 로고    scopus 로고
    • The complexities of p97 function in health and disease
    • Chapman, E., Fry, A. N., and Kang, M. (2011) The complexities of p97 function in health and disease. Mol. Biosyst. 7, 700-710
    • (2011) Mol. Biosyst. , vol.7 , pp. 700-710
    • Chapman, E.1    Fry, A.N.2    Kang, M.3
  • 8
    • 79952834859 scopus 로고    scopus 로고
    • P97-containing complexes in proliferation control and cancer: Emerging culprits or guilt by association?
    • Haines, D. S. (2010) p97-containing complexes in proliferation control and cancer: emerging culprits or guilt by association? Genes Cancer 1, 753-763
    • (2010) Genes Cancer , vol.1 , pp. 753-763
    • Haines, D.S.1
  • 10
    • 80052353713 scopus 로고    scopus 로고
    • Development of p97 AAA ATPase inhibitors
    • Chou, T. F., and Deshaies, R. J. (2011) Development of p97 AAA ATPase inhibitors. Autophagy 7, 1091-1092
    • (2011) Autophagy , vol.7 , pp. 1091-1092
    • Chou, T.F.1    Deshaies, R.J.2
  • 12
  • 13
    • 49249130739 scopus 로고    scopus 로고
    • UBX domain proteins: Major regulators of the AAA ATPase Cdc48/p97
    • Schuberth, C., and Buchberger, A. (2008) UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97. Cell Mol. Life Sci. 65, 2360-2371
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 2360-2371
    • Schuberth, C.1    Buchberger, A.2
  • 14
    • 73349115264 scopus 로고    scopus 로고
    • A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor-promoter DNA complex
    • Wilcox, A. J., and Laney, J. D. (2009) A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor-promoter DNA complex. Nat. Cell Biol. 11, 1481-1486
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1481-1486
    • Wilcox, A.J.1    Laney, J.D.2
  • 15
    • 84873909937 scopus 로고    scopus 로고
    • The budding yeast Cdc48 (Shp1) complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (Glc7)
    • Böhm, S., and Buchberger, A. (2013) The budding yeast Cdc48 (Shp1) complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (Glc7). PLoS One 8, e56486
    • (2013) PLoS One , vol.8
    • Böhm, S.1    Buchberger, A.2
  • 16
    • 84874899260 scopus 로고    scopus 로고
    • Ubiquitination of the N-terminal Region of Caveolin-1 Regulates Endosomal Sorting by the VCP/p97 AAA-ATPase
    • Kirchner, P., Bug, M., and Meyer, H. (2013) Ubiquitination of the N-terminal Region of Caveolin-1 Regulates Endosomal Sorting by the VCP/p97 AAA-ATPase. J. Biol. Chem. 288, 7363-7372
    • (2013) J. Biol. Chem. , vol.288 , pp. 7363-7372
    • Kirchner, P.1    Bug, M.2    Meyer, H.3
  • 17
    • 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
  • 18
    • 78650733298 scopus 로고    scopus 로고
    • Cdc48/p97 mediates UV-dependent turnover of RNA Pol II
    • Verma, R., Oania, R., Fang, R., Smith, G. T., and Deshaies, R. J. (2011) Cdc48/p97 mediates UV-dependent turnover of RNA Pol II. Mol. Cell 41, 82-92
    • (2011) Mol. Cell , vol.41 , pp. 82-92
    • Verma, R.1    Oania, R.2    Fang, R.3    Smith, G.T.4    Deshaies, R.J.5
  • 19
    • 84865712651 scopus 로고    scopus 로고
    • Fas-associated factor 1 is a scaffold protein that promotes beta-transducin repeat-containing protein (beta-TrCP)-mediated beta-catenin ubiquitination and degradation
    • Zhang, L., Zhou, F., Li, Y., Drabsch, Y., Zhang, J., van Dam, H., and ten Dijke, P. (2012) Fas-associated factor 1 is a scaffold protein that promotes beta-transducin repeat-containing protein (beta-TrCP)-mediated beta-catenin ubiquitination and degradation. J. Biol. Chem. 287, 30701-30710
    • (2012) J. Biol. Chem. , vol.287 , pp. 30701-30710
    • Zhang, L.1    Zhou, F.2    Li, Y.3    Drabsch, Y.4    Zhang, J.5    Van Dam, H.6    Ten Dijke, P.7
  • 20
    • 77950189379 scopus 로고    scopus 로고
    • The Cdc48-Ufd1-Npl4 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1, 6-bisphosphatase
    • Barbin, L., Eisele, F., Santt, O., and Wolf, D. H. (2010) The Cdc48-Ufd1-Npl4 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1, 6-bisphosphatase. Biochem. Biophys. Res. Commun. 394, 335-341
    • (2010) Biochem. Biophys. Res. Commun. , vol.394 , pp. 335-341
    • Barbin, L.1    Eisele, F.2    Santt, O.3    Wolf, D.H.4
  • 21
    • 84874871591 scopus 로고    scopus 로고
    • Complex of Fas-associated Factor 1 (FAF1) with Valosincontaining Protein (VCP)-Npl4-Ufd1 and Polyubiquitinated Proteins Promotes Endoplasmic Reticulum-associated Degradation (ERAD)
    • Lee, J. J., Park, J. K., Jeong, J., Jeon, H., Yoon, J. B., Kim, E. E., and Lee, K. J. (2013) Complex of Fas-associated Factor 1 (FAF1) with Valosincontaining Protein (VCP)-Npl4-Ufd1 and Polyubiquitinated Proteins Promotes Endoplasmic Reticulum-associated Degradation (ERAD). J. Biol. Chem. 288, 6998-7011
    • (2013) J. Biol. Chem. , vol.288 , pp. 6998-7011
    • Lee, J.J.1    Park, J.K.2    Jeong, J.3    Jeon, H.4    Yoon, J.B.5    Kim, E.E.6    Lee, K.J.7
  • 22
    • 84864419019 scopus 로고    scopus 로고
    • Ubiquitin-associated (UBA) domain in human Fas associated factor 1 inhibits tumor formation by promoting Hsp70 degradation
    • Lee, J. J., Kim, Y. M., Jeong, J., Bae, D. S., and Lee, K. J. (2012) Ubiquitin-associated (UBA) domain in human Fas associated factor 1 inhibits tumor formation by promoting Hsp70 degradation. PLoS One 7, e40361
    • (2012) PLoS One , vol.7
    • Lee, J.J.1    Kim, Y.M.2    Jeong, J.3    Bae, D.S.4    Lee, K.J.5
  • 23
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe, T., Matuschewski, K., Rape, M., Schlenker, S., Ulrich, H. D., and 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
  • 24
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48 (UFD1/NPL4), a ubiquitin-selective chaperone
    • Rape, M., Hoppe, T., Gorr, I., Kalocay, M., Richly, H., and Jentsch, S. (2001) Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48 (UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107, 667-677
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 25
    • 0034746779 scopus 로고    scopus 로고
    • The conserved npl4 protein complex mediates proteasomedependent membrane-bound transcription factor activation
    • Hitchcock, A. L., Krebber, H., Frietze, S., Lin, A., Latterich, M., and Silver, P. A. (2001) The conserved npl4 protein complex mediates proteasomedependent membrane-bound transcription factor activation. Mol. Biol. Cell 12, 3226-3241
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3226-3241
    • Hitchcock, A.L.1    Krebber, H.2    Frietze, S.3    Lin, A.4    Latterich, M.5    Silver, P.A.6
  • 26
    • 33947279970 scopus 로고    scopus 로고
    • Regulation of long chain unsaturated fatty acid synthesis in yeast
    • Martin, C. E., Oh, C. S., and Jiang, Y. (2007) Regulation of long chain unsaturated fatty acid synthesis in yeast. Biochim. Biophys. Acta 1771, 271-285
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 271-285
    • Martin, C.E.1    Oh, C.S.2    Jiang, Y.3
  • 27
    • 0032962409 scopus 로고    scopus 로고
    • MGA2 or SPT23 is required for transcription of the delta9 fatty acid desaturase gene, OLE1, and nuclear membrane integrity in Saccharomyces cerevisiae
    • Zhang, S., Skalsky, Y., and Garfinkel, D. J. (1999) MGA2 or SPT23 is required for transcription of the delta9 fatty acid desaturase gene, OLE1, and nuclear membrane integrity in Saccharomyces cerevisiae. Genetics 151, 473-483
    • (1999) Genetics , vol.151 , pp. 473-483
    • Zhang, S.1    Skalsky, Y.2    Garfinkel, D.J.3
  • 28
    • 0038376459 scopus 로고    scopus 로고
    • Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90
    • Shcherbik, N., Zoladek, T., Nickels, J. T., and Haines, D. S. (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
  • 29
    • 33746786326 scopus 로고    scopus 로고
    • Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site
    • Piwko, W., and Jentsch, S. (2006) Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site. Nat. Struct. Mol. Biol. 13, 691-697
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 691-697
    • Piwko, W.1    Jentsch, S.2
  • 30
    • 11144228252 scopus 로고    scopus 로고
    • A single PXY motif located within the carboxyl terminus of Spt23p and Mga2p mediates a physical and functional interaction with ubiquitin ligase Rsp5p
    • Shcherbik, N., Kee, Y., Lyon, N., Huibregtse, J. M., and Haines, D. S. (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
    • (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
  • 31
    • 33846705026 scopus 로고    scopus 로고
    • Cdc48p (Npl4p/Ufd1p) binds and segregates membrane-anchored/tethered complexes via a polyubiquitin signal present on the anchors
    • Shcherbik, N., and Haines, D. S. (2007) Cdc48p (Npl4p/Ufd1p) binds and segregates membrane-anchored/tethered complexes via a polyubiquitin signal present on the anchors. Mol. Cell 25, 385-397
    • (2007) Mol. Cell , vol.25 , pp. 385-397
    • Shcherbik, N.1    Haines, D.S.2
  • 32
    • 0037084028 scopus 로고    scopus 로고
    • Role of the ubiquitin-selective CDC48 (UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates
    • Braun, S., Matuschewski, K., Rape, M., Thoms, S., and Jentsch, S. (2002) Role of the ubiquitin-selective CDC48 (UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21, 615-621
    • (2002) EMBO J. , vol.21 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thoms, S.4    Jentsch, S.5
  • 33
    • 30744451400 scopus 로고    scopus 로고
    • Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone
    • Rumpf, S., and Jentsch, S. (2006) Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Mol. Cell 21, 261-269
    • (2006) Mol. Cell , vol.21 , pp. 261-269
    • Rumpf, S.1    Jentsch, S.2
  • 34
    • 4344700923 scopus 로고    scopus 로고
    • Regulation of unsaturated fatty acid biosynthesis in Saccharomyces: The -endoplasmic reticulum membrane protein, Mga2p, a transcription activator of the OLE1 gene, regulates the stability of the OLE1 mRNA through exosome-mediated mechanisms
    • Kandasamy, P., Vemula, M., Oh, C. S., Chellappa, R., and Martin, C. E. (2004) Regulation of unsaturated fatty acid biosynthesis in Saccharomyces: the -endoplasmic reticulum membrane protein, Mga2p, a transcription activator of the OLE1 gene, regulates the stability of the OLE1 mRNA through exosome-mediated mechanisms. J. Biol. Chem. 279, 36586-36592
    • (2004) J. Biol. Chem. , vol.279 , pp. 36586-36592
    • Kandasamy, P.1    Vemula, M.2    Oh, C.S.3    Chellappa, R.4    Martin, C.E.5
  • 35
    • 21044460108 scopus 로고    scopus 로고
    • Two-step affinity purification of multiubiquitylated proteins from Saccharomyces cerevisiae
    • Mayor, T., and Deshaies, R. J. (2005) Two-step affinity purification of multiubiquitylated proteins from Saccharomyces cerevisiae. Methods Enzymol. 399, 385-392
    • (2005) Methods Enzymol. , vol.399 , pp. 385-392
    • Mayor, T.1    Deshaies, R.J.2
  • 36
    • 79957637389 scopus 로고    scopus 로고
    • Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1
    • Gomez, T. A., Kolawa, N., Gee, M., Sweredoski, M. J., and Deshaies, R. J. (2011) Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1. BMC Biol. 9, 33
    • (2011) BMC Biol. , vol.9 , pp. 33
    • Gomez, T.A.1    Kolawa, N.2    Gee, M.3    Sweredoski, M.J.4    Deshaies, R.J.5
  • 37
    • 71549117585 scopus 로고    scopus 로고
    • Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome
    • Wiśniewski, J. R., Zougman, A., and Mann, M. (2009) Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome. J. Proteome Res. 8, 5674-5678
    • (2009) J. Proteome Res. , vol.8 , pp. 5674-5678
    • Wiśniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 39
    • 84855462699 scopus 로고    scopus 로고
    • Effect of mass spectrometric parameters on peptide and protein identification rates for shotgun proteomic experiments on an LTQ-orbitrap mass analyzer
    • Kalli, A., and Hess, S. (2012) Effect of mass spectrometric parameters on peptide and protein identification rates for shotgun proteomic experiments on an LTQ-orbitrap mass analyzer. Proteomics 12, 21-31
    • (2012) Proteomics , vol.12 , pp. 21-31
    • Kalli, A.1    Hess, S.2
  • 40
    • 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
  • 42
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da, W., Sherman, B. T., and Lempicki, R. A. (2009) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44-57
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Da Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 43
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists
    • Huang da, W., Sherman, B. T., and Lempicki, R. A. (2009) Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 37, 1-13
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1-13
    • Da Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 44
    • 0035829361 scopus 로고    scopus 로고
    • Controlling the false discovery rate in behavior genetics research
    • Benjamini, Y., Drai, D., Elmer, G., Kafkafi, N., and Golani, I. (2001) Controlling the false discovery rate in behavior genetics research. Behav. Brain Res. 125, 279-284
    • (2001) Behav. Brain Res. , vol.125 , pp. 279-284
    • Benjamini, Y.1    Drai, D.2    Elmer, G.3    Kafkafi, N.4    Golani, I.5
  • 45
    • 1242341446 scopus 로고    scopus 로고
    • Binding of Cdc48p to a ubiquitin-related UBX domain from novel yeast proteins involved in intracellular proteolysis and sporulation
    • Decottignies, A., Evain, A., and Ghislain, M. (2004) Binding of Cdc48p to a ubiquitin-related UBX domain from novel yeast proteins involved in intracellular proteolysis and sporulation. Yeast 21, 127-139
    • (2004) Yeast , vol.21 , pp. 127-139
    • Decottignies, A.1    Evain, A.2    Ghislain, M.3
  • 46
    • 44849131929 scopus 로고    scopus 로고
    • Feedback regulation of cholesterol synthesis: Sterol-accelerated ubiquitination and degradation of HMG CoA reductase
    • DeBose-Boyd, R. A. (2008) Feedback regulation of cholesterol synthesis: sterol-accelerated ubiquitination and degradation of HMG CoA reductase. Cell Res. 18, 609-621
    • (2008) Cell Res. , vol.18 , pp. 609-621
    • DeBose-Boyd, R.A.1
  • 49
    • 84860120476 scopus 로고    scopus 로고
    • UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1alpha accumulation
    • Bandau, S., Knebel, A., Gage, Z. O., Wood, N. T., and Alexandru, G. (2012) UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1alpha accumulation. BMC Biol. 10, 36
    • (2012) BMC Biol. , vol.10 , pp. 36
    • Bandau, S.1    Knebel, A.2    Gage, Z.O.3    Wood, N.T.4    Alexandru, G.5
  • 50
    • 0024424620 scopus 로고
    • Isolation and characterization of OLE1, a gene affecting fatty acid desaturation from Saccharomyces cerevisiae
    • Stukey, J. E., McDonough, V. M., and Martin, C. E. (1989) Isolation and characterization of OLE1, a gene affecting fatty acid desaturation from Saccharomyces cerevisiae. J. Biol. Chem. 264, 16537-16544
    • (1989) J. Biol. Chem. , vol.264 , pp. 16537-16544
    • Stukey, J.E.1    McDonough, V.M.2    Martin, C.E.3
  • 51
    • 22744456248 scopus 로고    scopus 로고
    • The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme
    • Kee, Y., Lyon, N., and Huibregtse, J. M. (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.M.3
  • 52
    • 33845939821 scopus 로고    scopus 로고
    • Cdc48 (p97): A "molecular gearbox" in the ubiquitin pathway?
    • Jentsch, S., and Rumpf, S. (2007) Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway? Trends Biochem. Sci. 32, 6-11
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 6-11
    • Jentsch, S.1    Rumpf, S.2
  • 53
    • 84867426217 scopus 로고    scopus 로고
    • The ubiquitin-like (UBX)-domaincontaining protein Ubx2/Ubxd8 regulates lipid droplet homeostasis
    • Wang, C. W., and Lee, S. C. (2012) The ubiquitin-like (UBX)-domaincontaining protein Ubx2/Ubxd8 regulates lipid droplet homeostasis. J. Cell Sci. 125, 2930-2939
    • (2012) J. Cell Sci. , vol.125 , pp. 2930-2939
    • Wang, C.W.1    Lee, S.C.2
  • 54
    • 57749114764 scopus 로고    scopus 로고
    • Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiquitination step
    • Lee, J. N., Zhang, X., Feramisco, J. D., Gong, Y., and Ye, J. (2008) Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiquitination step. J. Biol. Chem. 283, 33772-33783
    • (2008) J. Biol. Chem. , vol.283 , pp. 33772-33783
    • Lee, J.N.1    Zhang, X.2    Feramisco, J.D.3    Gong, Y.4    Ye, J.5
  • 55
    • 78650718129 scopus 로고    scopus 로고
    • Identification of Ubxd8 protein as a sensor for unsaturated fatty acids and regulator of triglyceride synthesis
    • Lee, J. N., Kim, H., Yao, H., Chen, Y., Weng, K., and Ye, J. (2010) Identification of Ubxd8 protein as a sensor for unsaturated fatty acids and regulator of triglyceride synthesis. Proc. Natl. Acad. Sci. U. S. A. 107, 21424-21429
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 21424-21429
    • Lee, J.N.1    Kim, H.2    Yao, H.3    Chen, Y.4    Weng, K.5    Ye, J.6
  • 56
    • 79952995078 scopus 로고    scopus 로고
    • The UBX protein SAKS1 negatively regulates endoplasmic reticulum-associated degradation and p97-dependent degradation
    • LaLonde, D. P., and Bretscher, A. (2011) The UBX protein SAKS1 negatively regulates endoplasmic reticulum-associated degradation and p97-dependent degradation. J. Biol. Chem. 286, 4892-4901
    • (2011) J. Biol. Chem. , vol.286 , pp. 4892-4901
    • LaLonde, D.P.1    Bretscher, A.2
  • 57
    • 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
  • 58
    • 84875242776 scopus 로고    scopus 로고
    • Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains
    • Volmer, R., van der Ploeg, K., and Ron, D. (2013) Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains. Proc. Natl. Acad. Sci. U. S. A. 110, 4628-4633
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 4628-4633
    • Volmer, R.1    Van Der Ploeg, K.2    Ron, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.