메뉴 건너뛰기




Volumn 4, Issue 3, 2014, Pages 646-661

Protein quality control in the nucleus

Author keywords

Chaperone; Degradation; Misfolding; Proteasome; Stress; SUMO; Ubiquitin

Indexed keywords

CHAPERONE; FUNGAL PROTEIN; NUCLEAR PROTEIN; SUMO PROTEIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 84930354120     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom4030646     Document Type: Review
Times cited : (34)

References (87)
  • 1
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl, F.U.; Hayer-Hartl, M. Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 2009, 16, 574-581.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 3
    • 77952851112 scopus 로고    scopus 로고
    • Chaperone-assisted degradation: Multiple paths to destruction
    • Kettern, N.; Dreiseidler, M.; Tawo, R.; Hohfeld, J. Chaperone-assisted degradation: Multiple paths to destruction. Biol. Chem. 2010, 391, 481-489.
    • (2010) Biol. Chem. , vol.391 , pp. 481-489
    • Kettern, N.1    Dreiseidler, M.2    Tawo, R.3    Hohfeld, J.4
  • 4
    • 9644280977 scopus 로고    scopus 로고
    • Cooperation of molecular chaperones with the ubiquitin/proteasome system
    • Esser, C.; Alberti, S.; Hohfeld, J. Cooperation of molecular chaperones with the ubiquitin/proteasome system. Biochim. Biophys. Acta 2004, 1695, 171-188.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 171-188
    • Esser, C.1    Alberti, S.2    Hohfeld, J.3
  • 5
    • 79954511326 scopus 로고    scopus 로고
    • Redox control of the ubiquitin-proteasome system: From molecular mechanisms to functional significance
    • Kriegenburg, F.; Poulsen, E.G.; Koch, A.; Kruger, E.; Hartmann-Petersen, R. Redox control of the ubiquitin-proteasome system: From molecular mechanisms to functional significance. Antioxid. Redox Signal. 2011, 15, 2265-2299.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 2265-2299
    • Kriegenburg, F.1    Poulsen, E.G.2    Koch, A.3    Kruger, E.4    Hartmann-Petersen, R.5
  • 6
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein, D.C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006, 443, 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 7
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • Vembar, S.S.; Brodsky, J.L. One step at a time: Endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 2008, 9, 944-957.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 8
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone chip targets immature CFTR for proteasomal degradation
    • Meacham, G.C.; Patterson, C.; Zhang, W.; Younger, J.M.; Cyr, D.M. The Hsc70 co-chaperone chip targets immature CFTR for proteasomal degradation. Nat. Cell Biol. 2001, 3, 100-105.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 9
    • 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. 2009, 78, 477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 10
    • 77951651753 scopus 로고    scopus 로고
    • The family of ubiquitin-conjugating enzymes (E2s): Deciding between life and death of proteins
    • Van Wijk, S.J.; Timmers, H.T. The family of ubiquitin-conjugating enzymes (E2s): Deciding between life and death of proteins. FASEB J. 2010, 24, 981-993.
    • (2010) FASEB J. , vol.24 , pp. 981-993
    • Van Wijk, S.J.1    Timmers, H.T.2
  • 13
    • 84856323688 scopus 로고    scopus 로고
    • Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation
    • Kriegenburg, F.; Ellgaard, L.; Hartmann-Petersen, R. Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation. FEBS J. 2012, 279, 532-542.
    • (2012) FEBS J. , vol.279 , pp. 532-542
    • Kriegenburg, F.1    Ellgaard, L.2    Hartmann-Petersen, R.3
  • 14
    • 35648993510 scopus 로고    scopus 로고
    • To be, or not to be-Molecular chaperones in protein degradation
    • Arndt, V.; Rogon, C.; Hohfeld, J. To be, or not to be-Molecular chaperones in protein degradation. Cell. Mol. Life Sci. 2007, 64, 2525-2541.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2525-2541
    • Arndt, V.1    Rogon, C.2    Hohfeld, J.3
  • 15
    • 33645293437 scopus 로고    scopus 로고
    • CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70
    • Qian, S.B.; McDonough, H.; Boellmann, F.; Cyr, D.M.; Patterson, C. CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70. Nature 2006, 440, 551-555.
    • (2006) Nature , vol.440 , pp. 551-555
    • Qian, S.B.1    McDonough, H.2    Boellmann, F.3    Cyr, D.M.4    Patterson, C.5
  • 18
    • 80455176947 scopus 로고    scopus 로고
    • Misfolded proteins driven to destruction by Hul5
    • Finley, D. Misfolded proteins driven to destruction by Hul5. Nat. Cell Biol. 2011, 13, 1290-1292.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1290-1292
    • Finley, D.1
  • 21
    • 34249864120 scopus 로고    scopus 로고
    • A proteasome for all occasions
    • Hanna, J.; Finley, D. A proteasome for all occasions. FEBS Lett. 2007, 581, 2854-2861.
    • (2007) FEBS Lett. , vol.581 , pp. 2854-2861
    • Hanna, J.1    Finley, D.2
  • 24
    • 78549277226 scopus 로고    scopus 로고
    • Yeast deubiquitinase Ubp3 interacts with the 26S proteasome to facilitate Rad4 degradation
    • Mao, P.; Smerdon, M.J. Yeast deubiquitinase Ubp3 interacts with the 26S proteasome to facilitate Rad4 degradation. J. Biol. Chem. 2010, 285, 37542-37550.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37542-37550
    • Mao, P.1    Smerdon, M.J.2
  • 25
    • 84892865694 scopus 로고    scopus 로고
    • Sorting out the trash: The spatial nature of eukaryotic protein quality control
    • Sontag, E.M.; Vonk, W.I.; Frydman, J. Sorting out the trash: The spatial nature of eukaryotic protein quality control. Curr. Opin. Cell Biol. 2014, 26, 139-146.
    • (2014) Curr. Opin. Cell Biol. , vol.26 , pp. 139-146
    • Sontag, E.M.1    Vonk, W.I.2    Frydman, J.3
  • 26
    • 84890204277 scopus 로고    scopus 로고
    • Protein quality control and elimination of protein waste: The role of the ubiquitin-proteasome system
    • Amm, I.; Sommer, T.; Wolf, D.H. Protein quality control and elimination of protein waste: The role of the ubiquitin-proteasome system. Biochim. Biophys. Acta 2014, 1843, 182-196.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 182-196
    • Amm, I.1    Sommer, T.2    Wolf, D.H.3
  • 27
    • 84879920420 scopus 로고    scopus 로고
    • Polyq proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1P chaperone
    • Park, S.H.; Kukushkin, Y.; Gupta, R.; Chen, T.; Konagai, A.; Hipp, M.S.; Hayer-Hartl, M.; Hartl, F.U. Polyq proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1P chaperone. Cell 2013, 154, 134-145.
    • (2013) Cell , vol.154 , pp. 134-145
    • Park, S.H.1    Kukushkin, Y.2    Gupta, R.3    Chen, T.4    Konagai, A.5    Hipp, M.S.6    Hayer-Hartl, M.7    Hartl, F.U.8
  • 30
    • 67449107793 scopus 로고    scopus 로고
    • The ubiquitin ligase E6-AP is induced and recruited to aggresomes in response to proteasome inhibition and may be involved in the ubiquitination of Hsp70-bound misfolded proteins
    • Mishra, A.; Godavarthi, S.K.; Maheshwari, M.; Goswami, A.; Jana, N.R. The ubiquitin ligase E6-AP is induced and recruited to aggresomes in response to proteasome inhibition and may be involved in the ubiquitination of Hsp70-bound misfolded proteins. J. Biol. Chem. 2009, 284, 10537-10545.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10537-10545
    • Mishra, A.1    Godavarthi, S.K.2    Maheshwari, M.3    Goswami, A.4    Jana, N.R.5
  • 31
    • 20144366969 scopus 로고    scopus 로고
    • HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome
    • Westhoff, B.; Chapple, J.P.; van der Spuy, J.; Hohfeld, J.; Cheetham, M.E. HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr. Biol. 2005, 15, 1058-1064.
    • (2005) Curr. Biol. , vol.15 , pp. 1058-1064
    • Westhoff, B.1    Chapple, J.P.2    Van Der Spuy, J.3    Hohfeld, J.4    Cheetham, M.E.5
  • 32
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • Demand, J.; Alberti, S.; Patterson, C.; Hohfeld, J. Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr. Biol. 2001, 11, 1569-1577.
    • (2001) Curr. Biol. , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 33
    • 0037195907 scopus 로고    scopus 로고
    • Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
    • Alberti, S.; Demand, J.; Esser, C.; Emmerich, N.; Schild, H.; Hohfeld, J. Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J. Biol. Chem. 2002, 277, 45920-45927.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45920-45927
    • Alberti, S.1    Demand, J.2    Esser, C.3    Emmerich, N.4    Schild, H.5    Hohfeld, J.6
  • 35
    • 0038268188 scopus 로고    scopus 로고
    • Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins
    • Seeger, M.; Hartmann-Petersen, R.; Wilkinson, C.R.; Wallace, M.; Samejima, I.; Taylor, M.S.; Gordon, C. Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins. J. Biol. Chem. 2003, 278, 16791-16796.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16791-16796
    • Seeger, M.1    Hartmann-Petersen, R.2    Wilkinson, C.R.3    Wallace, M.4    Samejima, I.5    Taylor, M.S.6    Gordon, C.7
  • 38
    • 28644442088 scopus 로고    scopus 로고
    • BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP
    • Arndt, V.; Daniel, C.; Nastainczyk, W.; Alberti, S.; Hohfeld, J. BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Mol. Biol. Cell 2005, 16, 5891-5900.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5891-5900
    • Arndt, V.1    Daniel, C.2    Nastainczyk, W.3    Alberti, S.4    Hohfeld, J.5
  • 40
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu, W.; Marcu, M.; Yuan, X.; Mimnaugh, E.; Patterson, C.; Neckers, L. Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc. Natl. Acad. Sci. USA 2002, 99, 12847-12852.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12847-12852
    • Xu, W.1    Marcu, M.2    Yuan, X.3    Mimnaugh, E.4    Patterson, C.5    Neckers, L.6
  • 41
    • 13144292426 scopus 로고    scopus 로고
    • BAG-1 haplo-insufficiency impairs lung tumorigenesis
    • Gotz, R.; Kramer, B.W.; Camarero, G.; Rapp, U.R. BAG-1 haplo-insufficiency impairs lung tumorigenesis. BMC Cancer. 2004, doi: 10.1186/1471-2407-4-85.
    • (2004) BMC Cancer.
    • Gotz, R.1    Kramer, B.W.2    Camarero, G.3    Rapp, U.R.4
  • 42
    • 17644396667 scopus 로고    scopus 로고
    • Degradation-mediated protein quality control in the nucleus
    • Gardner, R.G.; Nelson, Z.W.; Gottschling, D.E. Degradation-mediated protein quality control in the nucleus. Cell 2005, 120, 803-815.
    • (2005) Cell , vol.120 , pp. 803-815
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 43
    • 79953907268 scopus 로고    scopus 로고
    • Nuclear protein quality is regulated by the ubiquitin-proteasome system through the activity of Ubc4 and San1 in fission yeast
    • Matsuo, Y.; Kishimoto, H.; Tanae, K.; Kitamura, K.; Katayama, S.; Kawamukai, M. Nuclear protein quality is regulated by the ubiquitin-proteasome system through the activity of Ubc4 and San1 in fission yeast. J. Biol. Chem. 2011, 286, 13775-13790.
    • (2011) J. Biol. Chem. , vol.286 , pp. 13775-13790
    • Matsuo, Y.1    Kishimoto, H.2    Tanae, K.3    Kitamura, K.4    Katayama, S.5    Kawamukai, M.6
  • 44
    • 0033060521 scopus 로고    scopus 로고
    • Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein
    • Bhattacharyya, J.; Das, K.P. Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein. J. Biol. Chem. 1999, 274, 15505-15509.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15505-15509
    • Bhattacharyya, J.1    Das, K.P.2
  • 45
    • 1642524277 scopus 로고    scopus 로고
    • Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: The N-terminal domail is important for oligomer assembly and the binding of unfolding proteins
    • Stromer, T.; Fischer, E.; Richter, K.; Haslbeck, M.; Buchner, J. Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: The N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. J. Biol. Chem. 2004, 279, 11222-11228.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11222-11228
    • Stromer, T.1    Fischer, E.2    Richter, K.3    Haslbeck, M.4    Buchner, J.5
  • 46
    • 70349470609 scopus 로고    scopus 로고
    • Substrate binding site flexibility of the small heat shock protein molecular chaperones
    • Jaya, N.; Garcia, V.; Vierling, E. Substrate binding site flexibility of the small heat shock protein molecular chaperones. Proc. Natl. Acad. Sci. USA 2009, 106, 15604-15609.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 15604-15609
    • Jaya, N.1    Garcia, V.2    Vierling, E.3
  • 47
    • 84875470741 scopus 로고    scopus 로고
    • Means of self-preservation: How an intrinsically disordered ubiquitin-protein ligase averts self-destruction
    • Fredrickson, E.K.; Clowes Candadai, S.V.; Tam, C.H.; Gardner, R.G. Means of self-preservation: How an intrinsically disordered ubiquitin-protein ligase averts self-destruction. Mol. Biol. Cell 2013, 24, 1041-1052.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1041-1052
    • Fredrickson, E.K.1    Clowes Candadai, S.V.2    Tam, C.H.3    Gardner, R.G.4
  • 48
    • 84899728488 scopus 로고    scopus 로고
    • Requirement for Cdc48/p97 in nuclear protein quality control degradation varies with the substrate and correlates with substrate insolubility
    • Gallagher, P.S.; Clowes Candadai, S.V.; Gardner, R.G. Requirement for Cdc48/p97 in nuclear protein quality control degradation varies with the substrate and correlates with substrate insolubility. J. Cell Sci. 2014, 127, 1980-1991.
    • (2014) J. Cell Sci. , vol.127 , pp. 1980-1991
    • Gallagher, P.S.1    Clowes Candadai, S.V.2    Gardner, R.G.3
  • 51
    • 75749101797 scopus 로고    scopus 로고
    • The ubiquitin ligase Hul5 promotes proteasomal processivity
    • Aviram, S.; Kornitzer, D. The ubiquitin ligase Hul5 promotes proteasomal processivity. Mol. Cell. Biol. 2010, 30, 985-994.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 985-994
    • Aviram, S.1    Kornitzer, D.2
  • 52
    • 80455122748 scopus 로고    scopus 로고
    • Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins
    • Fang, N.N.; Ng, A.H.; Measday, V.; Mayor, T. Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nat. Cell Biol. 2011, 13, 1344-1352.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1344-1352
    • Fang, N.N.1    Ng, A.H.2    Measday, V.3    Mayor, T.4
  • 55
    • 84889072454 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates
    • Chu, B.W.; Kovary, K.M.; Guillaume, J.; Chen, L.C.; Teruel, M.N.; Wandless, T.J. The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates. J. Biol. Chem. 2013, 288, 34575-34587.
    • (2013) J. Biol. Chem. , vol.288 , pp. 34575-34587
    • Chu, B.W.1    Kovary, K.M.2    Guillaume, J.3    Chen, L.C.4    Teruel, M.N.5    Wandless, T.J.6
  • 56
    • 33746208871 scopus 로고    scopus 로고
    • A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
    • Denic, V.; Quan, E.M.; Weissman, J.S. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 2006, 126, 349-359.
    • (2006) Cell , vol.126 , pp. 349-359
    • Denic, V.1    Quan, E.M.2    Weissman, J.S.3
  • 57
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
    • Carvalho, P.; Goder, V.; Rapoport, T.A. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 2006, 126, 361-373.
    • (2006) Cell , vol.126 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 58
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
    • Swanson, R.; Locher, M.; Hochstrasser, M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev. 2001, 15, 2660-2674.
    • (2001) Genes Dev. , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 59
    • 32544437041 scopus 로고    scopus 로고
    • Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
    • Ravid, T.; Kreft, S.G.; Hochstrasser, M. Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. EMBO J. 2006, 25, 533-543.
    • (2006) EMBO J. , vol.25 , pp. 533-543
    • Ravid, T.1    Kreft, S.G.2    Hochstrasser, M.3
  • 60
    • 33750349837 scopus 로고    scopus 로고
    • Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase
    • Deng, M.; Hochstrasser, M. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature 2006, 443, 827-831.
    • (2006) Nature , vol.443 , pp. 827-831
    • Deng, M.1    Hochstrasser, M.2
  • 61
    • 84055200360 scopus 로고    scopus 로고
    • Exposure of bipartite hydrophobic signal triggers nuclear quality control of Ndc10 at the endoplasmic reticulum/nuclear envelope
    • Furth, N.; Gertman, O.; Shiber, A.; Alfassy, O.S.; Cohen, I.; Rosenberg, M.M.; Doron, N.K.; Friedler, A.; Ravid, T. Exposure of bipartite hydrophobic signal triggers nuclear quality control of Ndc10 at the endoplasmic reticulum/nuclear envelope. Mol. Biol. Cell 2011, 22, 4726-4739.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4726-4739
    • Furth, N.1    Gertman, O.2    Shiber, A.3    Alfassy, O.S.4    Cohen, I.5    Rosenberg, M.M.6    Doron, N.K.7    Friedler, A.8    Ravid, T.9
  • 62
    • 84879625944 scopus 로고    scopus 로고
    • Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting
    • Shiber, A.; Breuer, W.; Brandeis, M.; Ravid, T. Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting. Mol. Biol. Cell 2013, 24, 2076-2087.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 2076-2087
    • Shiber, A.1    Breuer, W.2    Brandeis, M.3    Ravid, T.4
  • 65
    • 79959381925 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies a role for SUMO in protein quality control
    • Tatham, M.H.; Matic, I.; Mann, M.; Hay, R.T. Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci. Signal. 2011, doi: 10.1126/scisignal.2001484.
    • (2011) Sci. Signal.
    • Tatham, M.H.1    Matic, I.2    Mann, M.3    Hay, R.T.4
  • 66
    • 33750980980 scopus 로고    scopus 로고
    • Purification of the yeast Slx5-Slx8 protein complex and characterization of its DNA-binding activity
    • Yang, L.; Mullen, J.R.; Brill, S.J. Purification of the yeast Slx5-Slx8 protein complex and characterization of its DNA-binding activity. Nucleic Acids Res. 2006, 34, 5541-5551.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 5541-5551
    • Yang, L.1    Mullen, J.R.2    Brill, S.J.3
  • 67
  • 69
    • 36348964395 scopus 로고    scopus 로고
    • The yeast Hex3·Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation
    • Xie, Y.; Kerscher, O.; Kroetz, M.B.; McConchie, H.F.; Sung, P.; Hochstrasser, M. The yeast Hex3·Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. J. Biol. Chem. 2007, 282, 34176-34184.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34176-34184
    • Xie, Y.1    Kerscher, O.2    Kroetz, M.B.3    McConchie, H.F.4    Sung, P.5    Hochstrasser, M.6
  • 70
    • 33645222457 scopus 로고    scopus 로고
    • Genetic analysis connects Slx5 and Slx8 to the SUMO pathway in Saccharomyces cerevisiae
    • Wang, Z.; Jones, G.M.; Prelich, G. Genetic analysis connects Slx5 and Slx8 to the SUMO pathway in Saccharomyces cerevisiae. Genetics 2006, 172, 1499-1509.
    • (2006) Genetics , vol.172 , pp. 1499-1509
    • Wang, Z.1    Jones, G.M.2    Prelich, G.3
  • 71
    • 63049110916 scopus 로고    scopus 로고
    • Quality control of a transcriptional regulator by SUMO-targeted degradation
    • Wang, Z.; Prelich, G. Quality control of a transcriptional regulator by SUMO-targeted degradation. Mol. Cell. Biol. 2009, 29, 1694-1706.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1694-1706
    • Wang, Z.1    Prelich, G.2
  • 73
    • 84865074686 scopus 로고    scopus 로고
    • The cell biology of disease: Acute promyelocytic leukemia, arsenic, and PML bodies
    • De Thé, H.; le Bras, M.; Lallemand-Breitenbach, V. The cell biology of disease: Acute promyelocytic leukemia, arsenic, and PML bodies. J. Cell Biol. 2012, 198, 11-21.
    • (2012) J. Cell Biol. , vol.198 , pp. 11-21
    • De Thé, H.1    Le Bras, M.2    Lallemand-Breitenbach, V.3
  • 74
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi, R.; Pandolfi, P.P. Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev. Mol. Cell Biol. 2007, 8, 1006-1016.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 79
    • 84878986048 scopus 로고    scopus 로고
    • Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML degradation
    • Erker, Y.; Neyret-Kahn, H.; Seeler, J.S.; Dejean, A.; Atfi, A.; Levy, L. Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML degradation. Mol. Cell. Biol. 2013, 33, 2163-2177.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 2163-2177
    • Erker, Y.1    Neyret-Kahn, H.2    Seeler, J.S.3    Dejean, A.4    Atfi, A.5    Levy, L.6
  • 80
    • 0025050840 scopus 로고
    • The recognition component of the N-end rule pathway
    • Bartel, B.; Wunning, I.; Varshavsky, A. The recognition component of the N-end rule pathway. EMBO J. 1990, 9, 3179-3189.
    • (1990) EMBO J. , vol.9 , pp. 3179-3189
    • Bartel, B.1    Wunning, I.2    Varshavsky, A.3
  • 81
    • 57049182407 scopus 로고    scopus 로고
    • Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase UBR1
    • Eisele, F.; Wolf, D.H. Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase UBR1. FEBS Lett. 2008, 582, 4143-4146.
    • (2008) FEBS Lett. , vol.582 , pp. 4143-4146
    • Eisele, F.1    Wolf, D.H.2
  • 82
    • 75749101057 scopus 로고    scopus 로고
    • Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1
    • Heck, J.W.; Cheung, S.K.; Hampton, R.Y. Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc. Natl. Acad. Sci. USA 2010, 107, 1106-1111.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1106-1111
    • Heck, J.W.1    Cheung, S.K.2    Hampton, R.Y.3
  • 83
    • 77954178073 scopus 로고    scopus 로고
    • A nucleus-based quality control mechanism for cytosolic proteins
    • Prasad, R.; Kawaguchi, S.; Ng, D.T. A nucleus-based quality control mechanism for cytosolic proteins. Mol. Biol. Cell 2010, 21, 2117-2127.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2117-2127
    • Prasad, R.1    Kawaguchi, S.2    Ng, D.T.3
  • 84
    • 84872482670 scopus 로고    scopus 로고
    • The type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein
    • Summers, D.W.; Wolfe, K.J.; Ren, H.Y.; Cyr, D.M. The type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein. PLoS One 2013, 8, e52099.
    • (2013) PLoS One , vol.8
    • Summers, D.W.1    Wolfe, K.J.2    Ren, H.Y.3    Cyr, D.M.4
  • 85
    • 84880053272 scopus 로고    scopus 로고
    • Hsp70 targets a cytoplasmic quality control substrate to the san1p ubiquitin ligase
    • Guerriero, C.J.; Weiberth, K.F.; Brodsky, J.L. Hsp70 targets a cytoplasmic quality control substrate to the san1p ubiquitin ligase. J. Biol. Chem. 2013, 288, 18506-18520.
    • (2013) J. Biol. Chem. , vol.288 , pp. 18506-18520
    • Guerriero, C.J.1    Weiberth, K.F.2    Brodsky, J.L.3
  • 86
    • 84857751498 scopus 로고    scopus 로고
    • The Ubiquitin ligase Ubr11 is essential for oligopeptide utilization in the fission yeast Schizosaccharomyces pombe
    • Kitamura, K.; Nakase, M.; Tohda, H.; Takegawa, K. The Ubiquitin ligase Ubr11 is essential for oligopeptide utilization in the fission yeast Schizosaccharomyces pombe. Eukaryot. Cell 2012, 11, 302-310.
    • (2012) Eukaryot. Cell , vol.11 , pp. 302-310
    • Kitamura, K.1    Nakase, M.2    Tohda, H.3    Takegawa, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.