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Volumn 291, Issue 4, 2016, Pages 1664-1675

Cold temperature induces the reprogramming of proteolytic pathways in yeast

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; CELL MEMBRANES; TEMPERATURE;

EID: 84955505929     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.698662     Document Type: Article
Times cited : (10)

References (49)
  • 1
    • 84861867814 scopus 로고    scopus 로고
    • Ubiquitin and membrane protein turnover: From cradle to grave
    • MacGurn, J. A., Hsu, P. C., and Emr, S. D. (2012) Ubiquitin and membrane protein turnover: from cradle to grave. Annu. Rev. Biochem. 81, 231-259
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 231-259
    • MacGurn, J.A.1    Hsu, P.C.2    Emr, S.D.3
  • 2
    • 84890203542 scopus 로고    scopus 로고
    • Regulation of proteasome activity in health and disease
    • Schmidt, M., and Finley, D. (2014) Regulation of proteasome activity in health and disease. Biochim. Biophys. Acta 1843, 13-25
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 13-25
    • Schmidt, M.1    Finley, D.2
  • 3
    • 84870762133 scopus 로고    scopus 로고
    • The endoplasmic reticulum-associated degradation pathways of budding yeast
    • Thibault, G., and Ng, D. T. (2012) The endoplasmic reticulum-associated degradation pathways of budding yeast. Cold Spring Harb. Perspect. Biol. 4, a013193
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , pp. a013193
    • Thibault, G.1    Ng, D.T.2
  • 5
    • 84875231510 scopus 로고    scopus 로고
    • Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes?
    • Nathan, J. A., Kim, H. T., Ting, L., Gygi, S. P., and Goldberg, A. L. (2013) Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes? EMBO J. 32, 552-565
    • (2013) EMBO J. , vol.32 , pp. 552-565
    • Nathan, J.A.1    Kim, H.T.2    Ting, L.3    Gygi, S.P.4    Goldberg, A.L.5
  • 6
    • 0042205318 scopus 로고    scopus 로고
    • The role of ubiquitin in down-regulation and intracellular sorting of membrane proteins: Insights from yeast
    • Horák, J. (2003) The role of ubiquitin in down-regulation and intracellular sorting of membrane proteins: insights from yeast. Biochim. Biophys. Acta 1614, 139-155
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 139-155
    • Horák, J.1
  • 7
    • 55549102963 scopus 로고    scopus 로고
    • Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface
    • Lin, C. H., MacGurn, J. A., Chu, T., Stefan, C. J., and Emr, S. D. (2008) Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135, 714-725
    • (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
  • 8
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih, S. C., Katzmann, D. J., Schnell, J. D., Sutanto, M., Emr, S. D., and Hicke, L. (2002) Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat. Cell Biol. 4, 389-393
    • (2002) Nat. Cell Biol. , vol.4 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 9
    • 0036304360 scopus 로고    scopus 로고
    • The vps27p hse1p complex binds ubiquitin and mediates endosomal protein sorting
    • Bilodeau, P. S., Urbanowski, J. L., Winistorfer, S. C., and Piper, R. C. (2002) The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nat. Cell Biol. 4, 534-539
    • (2002) Nat. Cell Biol. , vol.4 , pp. 534-539
    • Bilodeau, P.S.1    Urbanowski, J.L.2    Winistorfer, S.C.3    Piper, R.C.4
  • 10
    • 0033786796 scopus 로고    scopus 로고
    • The doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways
    • Amerik, A. Y., Nowak, J., Swaminathan, S., and 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
  • 11
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chainbinding protein mcb1 is a component of the 26S proteasome in saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • van Nocker, S., Sadis, S., Rubin, D. M., Glickman, M., Fu, H., Coux, O., Wefes, I., Finley, D., and Vierstra, R. D. (1996) The multiubiquitin-chainbinding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16, 6020-6028
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6020-6028
    • Van Nocker, S.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 12
    • 0031890210 scopus 로고    scopus 로고
    • Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit mcb1
    • Fu, H., Sadis, S., Rubin, D. M., Glickman, M., van Nocker, S., Finley, D., and Vierstra, R. D. (1998) Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1. J. Biol. Chem. 273, 1970-1981
    • (1998) J. Biol. Chem. , vol.273 , pp. 1970-1981
    • Fu, H.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Van Nocker, S.5    Finley, D.6    Vierstra, R.D.7
  • 16
    • 3042677641 scopus 로고    scopus 로고
    • Rad23 and rpn10 serve as alternative ubiquitin receptors for the proteasome
    • Elsasser, S., Chandler-Militello, D., Müller, B., Hanna, J., and Finley, D. (2004) Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J. Biol. Chem. 279, 26817-26822
    • (2004) J. Biol. Chem. , vol.279 , pp. 26817-26822
    • Elsasser, S.1    Chandler-Militello, D.2    Müller, B.3    Hanna, J.4    Finley, D.5
  • 17
    • 60549107173 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
    • Saeki, Y., Kudo, T., Sone, T., Kikuchi, Y., Yokosawa, H., Toh-e, A., and Tanaka, K. (2009) Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome. EMBO J. 28, 359-371
    • (2009) EMBO J. , vol.28 , pp. 359-371
    • Saeki, Y.1    Kudo, T.2    Sone, T.3    Kikuchi, Y.4    Yokosawa, H.5    Toh-E, A.6    Tanaka, K.7
  • 18
    • 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
  • 19
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991) Getting started with yeast. Methods Enzymol. 194, 3-21
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 20
    • 84984933087 scopus 로고    scopus 로고
    • The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
    • Villén, J., and Gygi, S. P. (2008) The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry. Nat. Protoc. 3, 1630-1638
    • (2008) Nat. Protoc. , vol.3 , pp. 1630-1638
    • Villén, J.1    Gygi, S.P.2
  • 22
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber, J., Ishihama, Y., and Mann, M. (2003) Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem. 75, 663-670
    • (2003) Anal. Chem. , vol.75 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 24
    • 84904325891 scopus 로고    scopus 로고
    • MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes
    • McAlister, G. C., Nusinow, D. P., Jedrychowski, M. P., Wühr, M., Huttlin, E. L., Erickson, B. K., Rad, R., Haas, W., and Gygi, S. P. (2014) MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes. Anal. Chem. 86, 7150-7158
    • (2014) Anal. Chem. , vol.86 , pp. 7150-7158
    • McAlister, G.C.1    Nusinow, D.P.2    Jedrychowski, M.P.3    Wühr, M.4    Huttlin, E.L.5    Erickson, B.K.6    Rad, R.7    Haas, W.8    Gygi, S.P.9
  • 26
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E., and Gygi, S. P. (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4, 207-214
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 30
    • 34548546480 scopus 로고    scopus 로고
    • Regulation of copper-dependent endocytosis and vacuolar degradation of the yeast copper transporter, ctr1p, by the rsp5 ubiquitin ligase
    • Liu, J., Sitaram, A., and Burd, C. G. (2007) Regulation of copper-dependent endocytosis and vacuolar degradation of the yeast copper transporter, Ctr1p, by the Rsp5 ubiquitin ligase. Traffic 8, 1375-1384
    • (2007) Traffic , vol.8 , pp. 1375-1384
    • Liu, J.1    Sitaram, A.2    Burd, C.G.3
  • 31
    • 0032879814 scopus 로고    scopus 로고
    • Pleiotropic defects caused by loss of the proteasome-interacting factors rad23 and rpn10 of saccharomyces cerevisiae
    • Lambertson, D., Chen, L., and Madura, K. (1999) Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae. Genetics 153, 69-79
    • (1999) Genetics , vol.153 , pp. 69-79
    • Lambertson, D.1    Chen, L.2    Madura, K.3
  • 32
    • 84885012783 scopus 로고    scopus 로고
    • Large-scale identification of ubiquitination sites by mass spectrometry
    • Udeshi, N. D., Mertins, P., Svinkina, T., and Carr, S. A. (2013) Large-scale identification of ubiquitination sites by mass spectrometry. Nat. Protoc. 8, 1950-1960
    • (2013) Nat. Protoc. , vol.8 , pp. 1950-1960
    • Udeshi, N.D.1    Mertins, P.2    Svinkina, T.3    Carr, S.A.4
  • 33
    • 77949890050 scopus 로고    scopus 로고
    • Cross-talk between remodeling and de novo pathways maintains phospholipid balance through ubiquitination
    • Butler, P. L., and Mallampalli, R. K. (2010) Cross-talk between remodeling and de novo pathways maintains phospholipid balance through ubiquitination. J. Biol. Chem. 285, 6246-6258
    • (2010) J. Biol. Chem. , vol.285 , pp. 6246-6258
    • Butler, P.L.1    Mallampalli, R.K.2
  • 34
    • 70649112359 scopus 로고    scopus 로고
    • Arrestin-mediated endocytosis of yeast plasma membrane transporters
    • Nikko, E., and Pelham, H. R. (2009) Arrestin-mediated endocytosis of yeast plasma membrane transporters. Traffic 10, 1856-1867
    • (2009) Traffic , vol.10 , pp. 1856-1867
    • Nikko, E.1    Pelham, H.R.2
  • 35
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan, J. M., and Haguenauer-Tsapis, R. (1997) Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 16, 5847-5854
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 36
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L., and Helenius, A. (2003) Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4, 181-191
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 37
    • 0037131243 scopus 로고    scopus 로고
    • Role of rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • Verma, R., Aravind, L., Oania, R., McDonald, W. H., Yates, J. R., 3rd, Koonin, E. V., and Deshaies, R. J. (2002) Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611-615
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates, J.R.5    Koonin, E.V.6    Deshaies, R.J.7
  • 38
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T., and Cohen, R. E. (2002) A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403-407
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 39
    • 11244343965 scopus 로고    scopus 로고
    • Rpn4 is a physiological substrate of the ubr2 ubiquitin ligase
    • Wang, L., Mao, X., Ju, D., and Xie, Y. (2004) Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase. J. Biol. Chem. 279, 55218-55223
    • (2004) J. Biol. Chem. , vol.279 , pp. 55218-55223
    • Wang, L.1    Mao, X.2    Ju, D.3    Xie, Y.4
  • 41
    • 39149132089 scopus 로고    scopus 로고
    • ESCRT complexes and the biogenesis of multivesicular bodies
    • Hurley, J. H. (2008) ESCRT complexes and the biogenesis of multivesicular bodies. Curr. Opin. Cell Biol. 20, 4-11
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 4-11
    • Hurley, J.H.1
  • 42
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence, J., Sadis, S., Haas, A. L., and Finley, D. (1995) A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 15, 1265-1273
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 43
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg, C., and Stenmark, H. (2009) The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458, 445-452
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 46
    • 37048999147 scopus 로고    scopus 로고
    • Acclimation of saccharomyces cerevisiae to low temperature: A chemostat-based transcriptome analysis
    • Tai, S. L., Daran-Lapujade, P., Walsh, M. C., Pronk, J. T., and Daran, J. M. (2007) Acclimation of Saccharomyces cerevisiae to low temperature: a chemostat-based transcriptome analysis. Mol. Biol. Cell 18, 5100-5112
    • (2007) Mol. Biol. Cell , vol.18 , pp. 5100-5112
    • Tai, S.L.1    Daran-Lapujade, P.2    Walsh, M.C.3    Pronk, J.T.4    Daran, J.M.5
  • 47
    • 77954203152 scopus 로고    scopus 로고
    • Metabolic pathway relationships revealed by an integrative analysis of the transcriptional and metabolic temperature stress-response dynamics in yeast
    • Walther, D., Strassburg, K., Durek, P., and Kopka, J. (2010) Metabolic pathway relationships revealed by an integrative analysis of the transcriptional and metabolic temperature stress-response dynamics in yeast. Omics 14, 261-274
    • (2010) Omics , vol.14 , pp. 261-274
    • Walther, D.1    Strassburg, K.2    Durek, P.3    Kopka, J.4
  • 48
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., Davies, A., Cost, G. J., Caputo, E., Li, J., Hieter, P., and Boeke, J. D. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14, 115-132
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 49
    • 0033168717 scopus 로고    scopus 로고
    • Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly
    • Arendt, C.S., and Hochstrasser, M. (1999) Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. EMBO J. 18, 3575-3585
    • (1999) EMBO J. , vol.18 , pp. 3575-3585
    • Arendt, C.S.1    Hochstrasser, M.2


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