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Volumn 536, Issue 7615, 2016, Pages 184-189

An evolutionarily conserved pathway controls proteasome homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MITOGEN ACTIVATED PROTEIN KINASE 7; MITOGEN ACTIVATED PROTEIN KINASE MPK1; PROTEASOME; REGULATORY PARTICLE ASSEMBLY CHAPERONE; UNCLASSIFIED DRUG; ADC17 PROTEIN, S CEREVISIAE; MITOGEN ACTIVATED PROTEIN KINASE; MTOR PROTEIN, HUMAN; PROTEIN SUBUNIT; SACCHAROMYCES CEREVISIAE PROTEIN; SLT2 PROTEIN, S CEREVISIAE; TARGET OF RAPAMYCIN KINASE; TORC1 PROTEIN COMPLEX, S CEREVISIAE; TRANSCRIPTION FACTOR;

EID: 84982094835     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature18943     Document Type: Article
Times cited : (150)

References (41)
  • 1
    • 33847066706 scopus 로고    scopus 로고
    • Functions of the proteasome: From protein degradation and immune surveillance to cancer therapy
    • Goldberg, A. L. Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochem. Soc. Trans. 35, 12-17 (2007).
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 12-17
    • Goldberg, A.L.1
  • 2
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477-513 (2009).
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 3
    • 84859827831 scopus 로고    scopus 로고
    • The proteasome: Molecular machinery and pathophysiological roles
    • Tanaka, K., Mizushima, T. & Saeki, Y. The proteasome: molecular machinery and pathophysiological roles. Biol. Chem. 393, 217-234 (2012).
    • (2012) Biol. Chem , vol.393 , pp. 217-234
    • Tanaka, K.1    Mizushima, T.2    Saeki, Y.3
  • 4
    • 84878942836 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the eukaryotic proteasome
    • Tomko, R. J. Jr & Hochstrasser, M. Molecular architecture and assembly of the eukaryotic proteasome. Annu. Rev. Biochem. 82, 415-445 (2013).
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 415-445
    • Tomko, R.J.1    Hochstrasser, M.2
  • 5
    • 59849083960 scopus 로고    scopus 로고
    • Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome
    • Le Tallec, B., Barrault, M. B., Guérois, R., Carré, T. & Peyroche, A. Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome. Mol. Cell 33, 389-399 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 389-399
    • Le Tallec, B.1    Barrault, M.B.2    Guérois, R.3    Carré, T.4    Peyroche, A.5
  • 6
    • 65849101541 scopus 로고    scopus 로고
    • Multiple proteasomeinteracting proteins assist the assembly of the yeast 19S regulatory particle
    • Saeki, Y., Toh-E, A., Kudo, T., Kawamura, H. & Tanaka, K. Multiple proteasomeinteracting proteins assist the assembly of the yeast 19S regulatory particle. Cell 137, 900-913 (2009).
    • (2009) Cell , vol.137 , pp. 900-913
    • Saeki, Y.1    Toh-E, A.2    Kudo, T.3    Kawamura, H.4    Tanaka, K.5
  • 7
    • 67349089027 scopus 로고    scopus 로고
    • Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base
    • Funakoshi, M., Tomko, R. J. Jr, Kobayashi, H. & Hochstrasser, M. Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell 137, 887-899 (2009).
    • (2009) Cell , vol.137 , pp. 887-899
    • Funakoshi, M.1    Tomko, R.J.2    Kobayashi, H.3    Hochstrasser, M.4
  • 8
    • 67149112112 scopus 로고    scopus 로고
    • Chaperone-mediated pathway of proteasome regulatory particle assembly
    • Roelofs, J. et al. Chaperone-mediated pathway of proteasome regulatory particle assembly. Nature 459, 861-865 (2009).
    • (2009) Nature , vol.459 , pp. 861-865
    • Roelofs, J.1
  • 9
    • 65849109465 scopus 로고    scopus 로고
    • Assembly pathway of the mammalian proteasome base subcomplex is mediated by multiple specific chaperones
    • Kaneko, T. et al. Assembly pathway of the mammalian proteasome base subcomplex is mediated by multiple specific chaperones. Cell 137, 914-925 (2009).
    • (2009) Cell , vol.137 , pp. 914-925
    • Kaneko, T.1
  • 10
    • 84906791334 scopus 로고    scopus 로고
    • An inducible chaperone adapts proteasome assembly to stress
    • Hanssum, A. et al. An inducible chaperone adapts proteasome assembly to stress. Mol. Cell 55, 566-577 (2014).
    • (2014) Mol. Cell , vol.55 , pp. 566-577
    • Hanssum, A.1
  • 11
    • 76749152448 scopus 로고    scopus 로고
    • The unfolded protein response
    • Wiseman, R. L., Haynes, C. M. & Ron, D. SnapShot: The unfolded protein response. Cell 140, 590-590.e2 (2010).
    • (2010) Cell , vol.140 , pp. 590-590e2
    • Wiseman, R.L.1    Haynes, C.M.2    SnapShot, R.D.3
  • 12
    • 79951493843 scopus 로고    scopus 로고
    • A comprehensive genomic binding map of gene and chromatin regulatory proteins in Saccharomyces
    • Venters, B. J. et al. A comprehensive genomic binding map of gene and chromatin regulatory proteins in Saccharomyces. Mol. Cell 41, 480-492 (2011).
    • (2011) Mol. Cell , vol.41 , pp. 480-492
    • Venters, B.J.1
  • 13
    • 5144229125 scopus 로고    scopus 로고
    • Sfp1 is a stress- and nutrient-sensitive regulator of ribosomal protein gene expression
    • Marion, R. M. et al. Sfp1 is a stress- and nutrient-sensitive regulator of ribosomal protein gene expression. Proc. Natl Acad. Sci. USA 101, 14315-14322 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 14315-14322
    • Marion, R.M.1
  • 14
    • 5444256434 scopus 로고    scopus 로고
    • A dynamic transcriptional network communicates growth potential to ribosome synthesis and critical cell size
    • Jorgensen, P. et al. A dynamic transcriptional network communicates growth potential to ribosome synthesis and critical cell size. Genes Dev. 18, 2491-2505 (2004).
    • (2004) Genes Dev , vol.18 , pp. 2491-2505
    • Jorgensen, P.1
  • 15
    • 62549119989 scopus 로고    scopus 로고
    • Sfp1 interaction with TORC1 and Mrs6 reveals feedback regulation on TOR signaling
    • Lempiäinen, H. et al. Sfp1 interaction with TORC1 and Mrs6 reveals feedback regulation on TOR signaling. Mol. Cell 33, 704-716 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 704-716
    • Lempiäinen, H.1
  • 16
    • 84864308260 scopus 로고    scopus 로고
    • Transient sequestration of TORC1 into stress granules during heat stress
    • Takahara, T. & Maeda, T. Transient sequestration of TORC1 into stress granules during heat stress. Mol. Cell 47, 242-252 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 242-252
    • Takahara, T.1    Maeda, T.2
  • 17
    • 34147133469 scopus 로고    scopus 로고
    • SnapShot: MTOR signaling
    • Soulard, A. & Hall, M. N. SnapShot: mTOR signaling. Cell 129, 434.e1-434.e2 (2007).
    • (2007) Cell , vol.129 , pp. 434e1-434e2
    • Soulard, A.1    Hall, M.N.2
  • 18
    • 83455177213 scopus 로고    scopus 로고
    • Target of rapamycin (TOR) in nutrient signaling and growth control
    • Loewith, R. & Hall, M. N. Target of rapamycin (TOR) in nutrient signaling and growth control. Genetics 189, 1177-1201 (2011).
    • (2011) Genetics , vol.189 , pp. 1177-1201
    • Loewith, R.1    Hall, M.N.2
  • 19
    • 78650510609 scopus 로고    scopus 로고
    • MTOR: From growth signal integration to cancer, diabetes and ageing
    • Zoncu, R., Efeyan, A. & Sabatini, D. M. mTOR: from growth signal integration to cancer, diabetes and ageing. Nature Rev. Mol. Cell Biol. 12, 21-35 (2011).
    • (2011) Nature Rev. Mol. Cell Biol , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 20
    • 0141764710 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase stimulation of Ca2+ signaling is required for survival of endoplasmic reticulum stress in yeast
    • Bonilla, M. & Cunningham, K. W. Mitogen-activated protein kinase stimulation of Ca2+ signaling is required for survival of endoplasmic reticulum stress in yeast. Mol. Biol. Cell 14, 4296-4305 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4296-4305
    • Bonilla, M.1    Cunningham, K.W.2
  • 21
    • 0037006802 scopus 로고    scopus 로고
    • The protein kinase C pathway is required for viability in quiescence in Saccharomyces cerevisiae
    • Krause, S. A. & Gray, J. V. The protein kinase C pathway is required for viability in quiescence in Saccharomyces cerevisiae. Curr. Biol. 12, 588-593 (2002).
    • (2002) Curr. Biol , vol.12 , pp. 588-593
    • Krause, S.A.1    Gray, J.V.2
  • 22
    • 0037044801 scopus 로고    scopus 로고
    • Regulation of the cell integrity pathway by rapamycin-sensitive TOR function in budding yeast
    • Torres, J., Di Como, C. J., Herrero, E. & De La Torre-Ruiz, M. A. Regulation of the cell integrity pathway by rapamycin-sensitive TOR function in budding yeast. J. Biol. Chem. 277, 43495-43504 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 43495-43504
    • Torres, J.1    Di Como, C.J.2    Herrero, E.3    De La Torre-Ruiz, M.A.4
  • 23
    • 77955051681 scopus 로고    scopus 로고
    • A surveillance pathway monitors the fitness of the endoplasmic reticulum to control its inheritance
    • Babour, A., Bicknell, A. A., Tourtellotte, J. & Niwa, M. A surveillance pathway monitors the fitness of the endoplasmic reticulum to control its inheritance. Cell 142, 256-269 (2010).
    • (2010) Cell , vol.142 , pp. 256-269
    • Babour, A.1    Bicknell, A.A.2    Tourtellotte, J.3    Niwa, M.4
  • 24
    • 83455179434 scopus 로고    scopus 로고
    • Regulation of cell wall biogenesis in Saccharomyces cerevisiae: The cell wall integrity signaling pathway
    • Levin, D. E. Regulation of cell wall biogenesis in Saccharomyces cerevisiae: the cell wall integrity signaling pathway. Genetics 189, 1145-1175 (2011).
    • (2011) Genetics , vol.189 , pp. 1145-1175
    • Levin, D.E.1
  • 25
    • 27644554700 scopus 로고    scopus 로고
    • A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes
    • Hirano, Y. et al. A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes. Nature 437, 1381-1385 (2005).
    • (2005) Nature , vol.437 , pp. 1381-1385
    • Hirano, Y.1
  • 26
    • 34547838178 scopus 로고    scopus 로고
    • 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals
    • Le Tallec, B. et al. 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol. Cell 27, 660-674 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 660-674
    • Le Tallec, B.1
  • 27
    • 0035853037 scopus 로고    scopus 로고
    • RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: A negative feedback circuit
    • Xie, Y. & Varshavsky, A. RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit. Proc. Natl Acad. Sci. USA 98, 3056-3061 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3056-3061
    • Xie, Y.1    Varshavsky, A.2
  • 28
    • 84868148725 scopus 로고    scopus 로고
    • Failure of amino acid homeostasis causes cell death following proteasome inhibition
    • Suraweera, A., Münch, C., Hanssum, A. & Bertolotti, A. Failure of amino acid homeostasis causes cell death following proteasome inhibition. Mol. Cell 48, 242-253 (2012).
    • (2012) Mol. Cell , vol.48 , pp. 242-253
    • Suraweera, A.1    Münch, C.2    Hanssum, A.3    Bertolotti, A.4
  • 29
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M. M., Finger, A., Schweiger, M. & Wolf, D. H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725-1728 (1996).
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 30
    • 4444320698 scopus 로고    scopus 로고
    • A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation
    • Medicherla, B., Kostova, Z., Schaefer, A. & Wolf, D. H. A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO Rep. 5, 692-697 (2004).
    • (2004) EMBO Rep , vol.5 , pp. 692-697
    • Medicherla, B.1    Kostova, Z.2    Schaefer, A.3    Wolf, D.H.4
  • 31
    • 84921752079 scopus 로고    scopus 로고
    • A molecular census of 26S proteasomes in intact neurons
    • Asano, S. et al. A molecular census of 26S proteasomes in intact neurons. Science 347, 439-442 (2015).
    • (2015) Science , vol.347 , pp. 439-442
    • Asano, S.1
  • 32
    • 33751184205 scopus 로고    scopus 로고
    • Expressed in the yeast Saccharomyces cerevisiae, human ERK5 is a client of the Hsp90 chaperone that complements loss of the Slt2p (Mpk1p) cell integrity stress-activated protein kinase
    • Truman, A. W. et al. Expressed in the yeast Saccharomyces cerevisiae, human ERK5 is a client of the Hsp90 chaperone that complements loss of the Slt2p (Mpk1p) cell integrity stress-activated protein kinase. Eukaryot. Cell 5, 1914-1924 (2006).
    • (2006) Eukaryot. Cell , vol.5 , pp. 1914-1924
    • Truman, A.W.1
  • 33
    • 84906898355 scopus 로고    scopus 로고
    • Coordinated regulation of protein synthesis and degradation by mTORC1
    • Zhang, Y. et al. Coordinated regulation of protein synthesis and degradation by mTORC1. Nature 513, 440-443 (2014).
    • (2014) Nature , vol.513 , pp. 440-443
    • Zhang, Y.1
  • 34
    • 84952705310 scopus 로고    scopus 로고
    • MTOR inhibition activates overall protein degradation by the ubiquitin proteasome system as well as by autophagy
    • Zhao, J., Zhai, B., Gygi, S. P. & Goldberg, A. L. mTOR inhibition activates overall protein degradation by the ubiquitin proteasome system as well as by autophagy. Proc. Natl Acad. Sci. USA 112, 15790-15797 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 15790-15797
    • Zhao, J.1    Zhai, B.2    Gygi, S.P.3    Goldberg, A.L.4
  • 35
    • 84930363624 scopus 로고    scopus 로고
    • MTOR signaling in cellular and organismal energetics
    • Albert, V. & Hall, M. N. mTOR signaling in cellular and organismal energetics. Curr. Opin. Cell Biol. 33, 55-66 (2015).
    • (2015) Curr. Opin. Cell Biol , vol.33 , pp. 55-66
    • Albert, V.1    Hall, M.N.2
  • 36
    • 33644792045 scopus 로고    scopus 로고
    • Yeast transformation by the LiAc/SS carrier DNA/ PEG method
    • Gietz, R. D. & Woods, R. A. Yeast transformation by the LiAc/SS carrier DNA/ PEG method. Methods Mol. Biol. 313, 107-120 (2006).
    • (2006) Methods Mol. Biol , vol.313 , pp. 107-120
    • Gietz, R.D.1    Woods, R.A.2
  • 37
    • 80255141913 scopus 로고    scopus 로고
    • An improved method for whole protein extraction from yeast Saccharomyces cerevisiae
    • Zhang, T. et al. An improved method for whole protein extraction from yeast Saccharomyces cerevisiae. Yeast 28, 795-798 (2011).
    • (2011) Yeast , vol.28 , pp. 795-798
    • Zhang, T.1
  • 38
    • 42449124168 scopus 로고    scopus 로고
    • Optimized protein extraction for quantitative proteomics of yeasts
    • von der Haar, T. Optimized protein extraction for quantitative proteomics of yeasts. PLoS One 2, e1078 (2007).
    • (2007) PLoS One , vol.2
    • Von Der Haar, T.1
  • 39
    • 34249813098 scopus 로고    scopus 로고
    • Sch9 is a major target of TORC1 in Saccharomyces cerevisiae
    • Urban, J. et al. Sch9 is a major target of TORC1 in Saccharomyces cerevisiae. Mol. Cell 26, 663-674 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 663-674
    • Urban, J.1
  • 40
    • 27644576445 scopus 로고    scopus 로고
    • Characterization of the proteasome using native gel electrophoresis
    • Elsasser, S., Schmidt, M. & Finley, D. Characterization of the proteasome using native gel electrophoresis. Methods Enzymol. 398, 353-363 (2005).
    • (2005) Methods Enzymol , vol.398 , pp. 353-363
    • Elsasser, S.1    Schmidt, M.2    Finley, D.3
  • 41
    • 79251584630 scopus 로고    scopus 로고
    • Domains of Tra1 important for activator recruitment and transcription coactivator functions of SAGA and NuA4 complexes
    • Knutson, B. A. & Hahn, S. Domains of Tra1 important for activator recruitment and transcription coactivator functions of SAGA and NuA4 complexes. Mol. Cell. Biol. 31, 818-831 (2011).
    • (2011) Mol. Cell. Biol , vol.31 , pp. 818-831
    • Knutson, B.A.1    Hahn, S.2


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