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Volumn 292, Issue 39, 2017, Pages 16333-16350

Dsc E3 ligase localization to the Golgi requires the ATPase Cdc48 and cofactor Ufd1 for activation of sterol regulatory element-binding protein in fission yeast

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; ALCOHOLS; CHEMICAL ACTIVATION; MASS SPECTROMETRY; OXYGEN; TRANSCRIPTION; YEAST;

EID: 85030033998     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M117.802025     Document Type: Article
Times cited : (6)

References (50)
  • 1
    • 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
  • 2
    • 84872021865 scopus 로고    scopus 로고
    • Deciphering the transcriptional-regulatory network of flocculation in Schizosaccharomyces pombe
    • Kwon, E. J., Laderoute, A., Chatfield-Reed, K., Vachon, L., Karagiannis, J., and Chua, G. (2012) Deciphering the transcriptional-regulatory network of flocculation in Schizosaccharomyces pombe. PLoS Genet. 8, e1003104
    • (2012) Plos Genet , vol.8
    • Kwon, E.J.1    Laderoute, A.2    Chatfield-Reed, K.3    Vachon, L.4    Karagiannis, J.5    Chua, G.6
  • 4
    • 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
  • 5
    • 84974694687 scopus 로고    scopus 로고
    • Mga2 transcription factor regulates an oxygen-responsive lipid homeostasis pathway in fission yeast
    • Burr, R., Stewart, E. V., Shao, W., Zhao, S., Hannibal-Bach, H. K., Ejsing, C. S., and Espenshade, P. J. (2016) Mga2 transcription factor regulates an oxygen-responsive lipid homeostasis pathway in fission yeast. J. Biol. Chem. 291, 12171–12183
    • (2016) J. Biol. Chem. , vol.291 , pp. 12171-12183
    • Burr, R.1    Stewart, E.V.2    Shao, W.3    Zhao, S.4    Hannibal-Bach, H.K.5    Ejsing, C.S.6    Espenshade, P.J.7
  • 7
    • 84980349624 scopus 로고    scopus 로고
    • Membrane-anchored ubiquitin ligase complex is required for the turnover of lysosomal membrane proteins
    • Li, M., Koshi, T., and Emr, S. D. (2015) Membrane-anchored ubiquitin ligase complex is required for the turnover of lysosomal membrane proteins. J. Cell Biol. 211, 639 – 652
    • (2015) J. Cell Biol. , vol.211 , pp. 639-652
    • Li, M.1    Koshi, T.2    Emr, S.D.3
  • 8
    • 84959508424 scopus 로고    scopus 로고
    • The signal peptide peptidase SppA is involved in sterol regulatory element-binding protein cleavage and hypoxia adaptation in Aspergillus nidulans
    • Bat-Ochir, C., Kwak, J. Y., Koh, S. K., Jeon, M. H., Chung, D., Lee, Y. W., and Chae, S. K. (2016) The signal peptide peptidase SppA is involved in sterol regulatory element-binding protein cleavage and hypoxia adaptation in Aspergillus nidulans. Mol. Microbiol. 100, 635– 655
    • (2016) Mol. Microbiol. , vol.100 , pp. 635-655
    • Bat-Ochir, C.1    Kwak, J.Y.2    Koh, S.K.3    Jeon, M.H.4    Chung, D.5    Lee, Y.W.6    Chae, S.K.7
  • 9
    • 84865389259 scopus 로고    scopus 로고
    • Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins
    • Fleig, L., Bergbold, N., Sahasrabudhe, P., Geiger, B., Kaltak, L., and Lemberg, M. K. (2012) Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins. Mol. Cell 47, 558 –569
    • (2012) Mol. Cell , vol.47 , pp. 558-569
    • Fleig, L.1    Bergbold, N.2    Sahasrabudhe, P.3    Geiger, B.4    Kaltak, L.5    Lemberg, M.K.6
  • 11
    • 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
  • 12
    • 84879034688 scopus 로고    scopus 로고
    • Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ri-bosome
    • Verma, R., Oania, R. S., Kolawa, N. J., and Deshaies, R. J. (2013) Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ri-bosome. eLife 2, e00308
    • (2013) Elife , vol.2 , pp. e00308
    • Verma, R.1    Oania, R.S.2    Kolawa, N.J.3    Deshaies, R.J.4
  • 13
    • 79955525976 scopus 로고    scopus 로고
    • Positive cooperativity of the p97 AAA ATPase is critical for essential functions
    • Nishikori, S., Esaki, M., Yamanaka, K., Sugimoto, S., and Ogura, T. (2011) Positive cooperativity of the p97 AAA ATPase is critical for essential functions. J. Biol. Chem. 286, 15815–15820
    • (2011) J. Biol. Chem. , vol.286 , pp. 15815-15820
    • Nishikori, S.1    Esaki, M.2    Yamanaka, K.3    Sugimoto, S.4    Ogura, T.5
  • 14
    • 85018732290 scopus 로고    scopus 로고
    • Molecular Mechanism of Substrate Processing by the Cdc48 ATPase Complex
    • Bodnar, N. O., and Rapoport, T. A. (2017) Molecular Mechanism of Substrate Processing by the Cdc48 ATPase Complex. Cell 169, 722–735
    • (2017) Cell , vol.169 , pp. 722-735
    • Bodnar, N.O.1    Rapoport, T.A.2
  • 16
    • 79953768271 scopus 로고    scopus 로고
    • Control of ubiquitin conjugation by cdc48 and its cofactors
    • Buchberger, A. (2010) Control of ubiquitin conjugation by cdc48 and its cofactors. Subcell. Biochem. 54, 17–30
    • (2010) Subcell. Biochem. , vol.54 , pp. 17-30
    • Buchberger, A.1
  • 17
    • 84995377027 scopus 로고    scopus 로고
    • A Dynamic molecular basis for malfunction in disease mutants of p97/VCP
    • Schuetz, A. K., and Kay, L. E. (2016) A Dynamic molecular basis for malfunction in disease mutants of p97/VCP. eLife 5, e20143
    • (2016) Elife , vol.5 , pp. e20143
    • Schuetz, A.K.1    Kay, L.E.2
  • 18
    • 84873699402 scopus 로고    scopus 로고
    • A unique IBMPFD-related P97/VCP mutation with differential binding pattern and subcellular localization
    • Erzurumlu, Y., Kose, F. A., Gozen, O., Gozuacik, D., Toth, E. A., and Ballar, P. (2013) A unique IBMPFD-related P97/VCP mutation with differential binding pattern and subcellular localization. Int. J. Biochem. Cell Biol. 45, 773–782
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 773-782
    • Erzurumlu, Y.1    Kose, F.A.2    Gozen, O.3    Gozuacik, D.4    Toth, E.A.5    Ballar, P.6
  • 19
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts, G. D., Wymer, J., Kovach, M. J., Mehta, S. G., Mumm, S., Darvish, D., Pestronk, A., Whyte, M. P., and Kimonis, V. E. (2004) Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat. Genet. 36, 377–381
    • (2004) Nat. Genet. , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3    Mehta, S.G.4    Mumm, S.5    Darvish, D.6    Pestronk, A.7    Whyte, M.P.8    Kimonis, V.E.9
  • 20
    • 84888356138 scopus 로고    scopus 로고
    • Different dynamic movements of wild-type and pathogenic VCPs and their cofactors to damaged mitochondria in a Parkin-mediated mitochondrial quality control system
    • Kimura, Y., Fukushi, J., Hori, S., Matsuda, N., Okatsu, K., Kakiyama, Y., Kawawaki, J., Kakizuka, A., and Tanaka, K. (2013) Different dynamic movements of wild-type and pathogenic VCPs and their cofactors to damaged mitochondria in a Parkin-mediated mitochondrial quality control system. Genes Cells 18, 1131–1143
    • (2013) Genes Cells , vol.18 , pp. 1131-1143
    • Kimura, Y.1    Fukushi, J.2    Hori, S.3    Matsuda, N.4    Okatsu, K.5    Kakiyama, Y.6    Kawawaki, J.7    Kakizuka, A.8    Tanaka, K.9
  • 23
    • 84863272299 scopus 로고    scopus 로고
    • The role of the N domain in the ATPase activity of the mammalian AAA ATPase p97/VCP
    • Niwa, H., Ewens, C. A., Tsang, C., Yeung, H. O., Zhang, X., and Freemont, P. S. (2012) The role of the N domain in the ATPase activity of the mammalian AAA ATPase p97/VCP. J. Biol. Chem. 287, 8561– 8570
    • (2012) J. Biol. Chem. , vol.287 , pp. 8561-8570
    • Niwa, H.1    Ewens, C.A.2    Tsang, C.3    Yeung, H.O.4    Zhang, X.5    Freemont, P.S.6
  • 25
    • 84880056038 scopus 로고    scopus 로고
    • Structural requirements for sterol regulatory element-binding protein (SREBP) cleavage in fission yeast
    • Cheung, R., and Espenshade, P. J. (2013) Structural requirements for sterol regulatory element-binding protein (SREBP) cleavage in fission yeast. J. Biol. Chem. 288, 20351–20360
    • (2013) J. Biol. Chem. , vol.288 , pp. 20351-20360
    • Cheung, R.1    Espenshade, P.J.2
  • 28
    • 84865475874 scopus 로고    scopus 로고
    • Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions
    • Nie, M., Aslanian, A., Prudden, J., Heideker, J., Vashisht, A. A., Wohlschlegel, J. A., Yates, J. R., 3rd., and Boddy, M. N. (2012) Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions. J. Biol. Chem. 287, 29610 –29619
    • (2012) J. Biol. Chem. , vol.287 , pp. 29610-29619
    • Nie, M.1    Aslanian, A.2    Prudden, J.3    Heideker, J.4    Vashisht, A.A.5    Wohlschlegel, J.A.6    Yates, J.R.7    Boddy, M.N.8
  • 29
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer, H. H., Shorter, J. G., Seemann, J., Pappin, D., and Warren, G. (2000) A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 19, 2181–2192
    • (2000) EMBO J. , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 30
    • 84855188325 scopus 로고    scopus 로고
    • The Cdc48 machine in endoplasmic reticulum associated protein degradation
    • Wolf, D. H., and Stolz, A. (2012) The Cdc48 machine in endoplasmic reticulum associated protein degradation. Biochim. Biophys. Acta 1823, 117–124
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 117-124
    • Wolf, D.H.1    Stolz, A.2
  • 31
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y., Meyer, H. H., and Rapoport, T. A. (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162, 71– 84
    • (2003) J. Cell Biol. , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 32
    • 9644255751 scopus 로고    scopus 로고
    • The AAA ATPase p97/VCP interacts with its alternative cofactors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism
    • Bruderer, R. M., Brasseur, C., and Meyer, H. H. (2004) The AAA ATPase p97/VCP interacts with its alternative cofactors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism. J. Biol. Chem. 279, 49609 – 49616
    • (2004) J. Biol. Chem. , vol.279 , pp. 49609-49616
    • Bruderer, R.M.1    Brasseur, C.2    Meyer, H.H.3
  • 33
    • 84930623337 scopus 로고    scopus 로고
    • Endoplasmic reticulum exit of Golgi-resident defective for SREBP cleavage (Dsc) E3 ligase complex requires its activity
    • Raychaudhuri, S., and Espenshade, P. J. (2015) Endoplasmic reticulum exit of Golgi-resident defective for SREBP cleavage (Dsc) E3 ligase complex requires its activity. J. Biol. Chem. 290, 14430 –14440
    • (2015) J. Biol. Chem. , vol.290 , pp. 14430-14440
    • Raychaudhuri, S.1    Espenshade, P.J.2
  • 34
    • 21744460209 scopus 로고    scopus 로고
    • Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
    • Park, S., Isaacson, R., Kim, H. T., Silver, P. A., and Wagner, G. (2005) Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 13, 995–1005
    • (2005) Structure , vol.13 , pp. 995-1005
    • Park, S.1    Isaacson, R.2    Kim, H.T.3    Silver, P.A.4    Wagner, G.5
  • 35
    • 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
  • 38
    • 85019969049 scopus 로고    scopus 로고
    • Ubiquitin- And ATP-dependent unfoldase activity of P97/VCP*NPLOC4*UFD1L is enhanced by a mutation that causes multisystem proteinopathy
    • Blythe, E. E., Olson, K. C., Chau, V., and Deshaies, R. J. (2017) Ubiquitin- and ATP-dependent unfoldase activity of P97/VCP*NPLOC4*UFD1L is enhanced by a mutation that causes multisystem proteinopathy. Proc. Natl. Acad. Sci. U.S.A. 114, E4380 –E4388
    • (2017) Proc. Natl. Acad. Sci. U.S.A. , vol.114 , pp. E4380-E4388
    • Blythe, E.E.1    Olson, K.C.2    Chau, V.3    Deshaies, R.J.4
  • 39
    • 34547464338 scopus 로고    scopus 로고
    • Ufd1 is a cofactor of gp78 and plays a key role in cholesterol metabolism by regulating the stability of HMG-CoA reductase
    • Cao, J., Wang, J., Qi, W., Miao, H. H., Wang, J., Ge, L., DeBose-Boyd, R. A., Tang, J. J., Li, B. L., and Song, B. L. (2007) Ufd1 is a cofactor of gp78 and plays a key role in cholesterol metabolism by regulating the stability of HMG-CoA reductase. Cell Metab. 6, 115–128
    • (2007) Cell Metab. , vol.6 , pp. 115-128
    • Cao, J.1    Wang, J.2    Qi, W.3    Miao, H.H.4    Wang, J.5    Ge, L.6    DeBose-Boyd, R.A.7    Tang, J.J.8    Li, B.L.9    Song, B.L.10
  • 40
    • 77953530388 scopus 로고    scopus 로고
    • Sterol-induced dislocation of 3-hy-droxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets
    • Hartman, I. Z., Liu, P., Zehmer, J. K., Luby-Phelps, K., Jo, Y., Anderson, R. G., and DeBose-Boyd, R. A. (2010) Sterol-induced dislocation of 3-hy-droxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets. J. Biol. Chem. 285, 19288 –19298
    • (2010) J. Biol. Chem. , vol.285 , pp. 19288-19298
    • Hartman, I.Z.1    Liu, P.2    Zehmer, J.K.3    Luby-Phelps, K.4    Jo, Y.5    Anderson, R.G.6    DeBose-Boyd, R.A.7
  • 41
    • 57749114764 scopus 로고    scopus 로고
    • Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiq-uitination 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 postubiq-uitination 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
  • 42
    • 56449097008 scopus 로고    scopus 로고
    • Insig regulates HMG-CoA reductase by controlling enzyme phosphorylation in fission yeast
    • Burg, J. S., Powell, D. W., Chai, R., Hughes, A. L., Link, A. J., and Espenshade, P. J. (2008) Insig regulates HMG-CoA reductase by controlling enzyme phosphorylation in fission yeast. Cell Metab. 8, 522–531
    • (2008) Cell Metab , vol.8 , pp. 522-531
    • Burg, J.S.1    Powell, D.W.2    Chai, R.3    Hughes, A.L.4    Link, A.J.5    Espenshade, P.J.6
  • 45
    • 52649138958 scopus 로고    scopus 로고
    • UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1 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 HIF1 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
    • 44349091967 scopus 로고    scopus 로고
    • Oxygen-regulated degradation of fission yeast SREBP by Ofd1, a prolyl hydroxylase family member
    • Hughes, B. T., and Espenshade, P. J. (2008) Oxygen-regulated degradation of fission yeast SREBP by Ofd1, a prolyl hydroxylase family member. EMBO J. 27, 1491–1501
    • (2008) EMBO J. , vol.27 , pp. 1491-1501
    • Hughes, B.T.1    Espenshade, P.J.2
  • 47
    • 2342511583 scopus 로고    scopus 로고
    • The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes
    • Hartmann-Petersen, R., Wallace, M., Hofmann, K., Koch, G., Johnsen, A. H., Hendil, K. B., and Gordon, C. (2004) The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes. Curr. Biol. 14, 824 – 828
    • (2004) Curr. Biol. , vol.14 , pp. 824-828
    • Hartmann-Petersen, R.1    Wallace, M.2    Hofmann, K.3    Koch, G.4    Johnsen, A.H.5    Hendil, K.B.6    Gordon, C.7
  • 48
    • 0027185274 scopus 로고
    • Comparison of Schizosaccharomyces pombe expression systems
    • Forsburg, S. L. (1993) Comparison of Schizosaccharomyces pombe expression systems. Nucleic Acids Res. 21, 2955–2956
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2955-2956
    • Forsburg, S.L.1
  • 49
    • 85016584234 scopus 로고    scopus 로고
    • Coordinate regulation of yeast sterol regulatory element-binding protein (SREBP) and Mga2 transcription factors
    • Burr, R., Stewart, E. V., and Espenshade, P. J. (2017) Coordinate regulation of yeast sterol regulatory element-binding protein (SREBP) and Mga2 transcription factors. J. Biol. Chem. 292, 5311–5324
    • (2017) J. Biol. Chem. , vol.292 , pp. 5311-5324
    • Burr, R.1    Stewart, E.V.2    Espenshade, P.J.3


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