DOI: 10.1016/j.molcel.2009.11.015. Ubiquitinated Proteins Activate the Proteasome by Binding to Usp14/Ubp6, which Causes 20S Gate Opening

Ubiquitinated Proteins Activate the Proteasome by Binding to Usp14/Ubp6, which Causes 20S Gate Opening

10.1016/j.molcel.2009.11.015

Crossref journal-article

Elsevier BV

Molecular Cell (78)

Bibliography

Peth, A., Besche, H. C., & Goldberg, A. L. (2009). Ubiquitinated Proteins Activate the Proteasome by Binding to Usp14/Ubp6, which Causes 20S Gate Opening. Molecular Cell, 36(5), 794â804.

Authors 3

Andreas Peth (first)
Henrike C. Besche (additional)
Alfred L. Goldberg (additional)

References 32 Referenced 189

10.1016/S0960-9822(03)00417-2 / Curr. Biol. / Proteasome disassembly and downregulation is correlated with viability during stationary phase by Bajorek (2003)
10.1038/nsmb.1547 / Nat. Struct. Mol. Biol. / Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome by Bech-Otschir (2009)
10.1016/S1097-2765(02)00775-X / Mol. Cell / ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation by Benaroudj (2003)
10.1021/bi802198q / Biochemistry / Isolation of mammalian 26S proteasomes and p97/VCP complexes using the ubiquitin-like domain from HHR23B reveals novel proteasome-associated proteins by Besche (2009)
10.1093/emboj/20.18.5187 / EMBO J. / A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14 by Borodovsky (2001)
10.1074/jbc.M404020200 / J. Biol. Chem. / Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome by Elsasser (2004)
10.1038/80992 / Nat. Struct. Biol. / A gated channel into the proteasome core particle by Groll (2000)
10.1038/sj.emboj.7601338 / EMBO J. / A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes by Hamazaki (2006)
10.1128/MCB.23.24.9251-9261.2003 / Mol. Cell. Biol. / Ubiquitin depletion as a key mediator of toxicity by translational inhibitors by Hanna (2003)
10.1016/j.cell.2006.07.038 / Cell / Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation by Hanna (2006)
10.1016/j.cell.2007.03.042 / Cell / A ubiquitin stress response induces altered proteasome composition by Hanna (2007)
10.1074/jbc.M103378200 / J. Biol. Chem. / In vitro assembly and recognition of Lys-63 polyubiquitin chains by Hofmann (2001)
10.1038/sj.emboj.7600832 / EMBO J. / Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14 by Hu (2005)
10.1038/nature06926 / Nature / Proteasome subunit Rpn13 is a novel ubiquitin receptor by Husnjak (2008)
10.1038/embor.2008.93 / EMBO Rep. / Atypical ubiquitin chains: new molecular signals. ‘Protein Modifications: Beyond the Usual Suspects’ review series by Ikeda (2008)
10.1074/jbc.M609659200 / J. Biol. Chem. / Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages by Kim (2007)
10.1074/jbc.M112360200 / J. Biol. Chem. / Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the alpha-rings by Kisselev (2002)
10.1016/S1097-2765(01)00274-X / Mol. Cell / The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release by Köhler (2001)
10.1038/385737a0 / Nature / Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome by Lam (1997)
10.1016/S1097-2765(02)00638-X / Mol. Cell / Multiple associated proteins regulate proteasome structure and function by Leggett (2002)
10.1042/BJ20090528 / Biochem. J. / Variably modulated gating of the 26S proteasome by ATP and polyubiquitin by Li (2009)
10.1016/S0021-9258(18)48117-3 / J. Biol. Chem. / Protein substrates activate the ATP-dependent protease La by promoting nucleotide binding and release of bound ADP by Menon (1987)
10.1038/nchembio.130 / Nat. Chem. Biol. / Substrate selection by the proteasome during degradation of protein complexes by Prakash (2009)
10.1016/j.molcel.2008.03.004 / Mol. Cell / Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases by Rabl (2008)
10.1093/emboj/17.17.4909 / EMBO J. / Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome by Rubin (1998)
10.1016/j.molcel.2005.10.019 / Mol. Cell / ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins by Smith (2005)
10.1016/j.molcel.2007.06.033 / Mol. Cell / Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry by Smith (2007)
10.1083/jcb.96.6.1580 / J. Cell Biol. / ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin by Tanaka (1983)
10.1093/emboj/19.1.94 / EMBO J. / Recognition of the polyubiquitin proteolytic signal by Thrower (2000)
10.1126/science.1075898 / Science / Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome by Verma (2002)
10.1126/science.2938257 / Science / Selectivity of intracellular proteolysis: protein substrates activate the ATP-dependent protease (La) by Waxman (1986)
10.1038/35040607 / Nature / Structural basis for the activation of 20S proteasomes by 11S regulators by Whitby (2000)

Dates

Type	When
Created	15 years, 8 months ago (Dec. 11, 2009, 10:11 a.m.)
Deposited	3 years, 10 months ago (Oct. 15, 2021, 7:18 p.m.)
Indexed	4 days, 22 hours ago (Aug. 19, 2025, 6 a.m.)
Issued	15 years, 8 months ago (Dec. 1, 2009)
Published	15 years, 8 months ago (Dec. 1, 2009)
Published Print	15 years, 8 months ago (Dec. 1, 2009)

Funders 0

None

BibTeX

@article{Peth_2009, title={Ubiquitinated Proteins Activate the Proteasome by Binding to Usp14/Ubp6, which Causes 20S Gate Opening}, volume={36}, ISSN={1097-2765}, url={http://dx.doi.org/10.1016/j.molcel.2009.11.015}, DOI={10.1016/j.molcel.2009.11.015}, number={5}, journal={Molecular Cell}, publisher={Elsevier BV}, author={Peth, Andreas and Besche, Henrike C. and Goldberg, Alfred L.}, year={2009}, month=dec, pages={794–804} }

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      "author": "Prakash",
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      "volume": "17",
      "author": "Rubin",
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      "volume": "20",
      "author": "Smith",
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      "volume": "96",
      "author": "Tanaka",
      "year": "1983",
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  "alternative-id": [
    "S1097276509008296"
  ],
  "URL": "http://dx.doi.org/10.1016/j.molcel.2009.11.015",
  "relation": {},
  "ISSN": [
    "1097-2765"
  ],
  "subject": [],
  "container-title-short": "Molecular Cell",
  "published": {
    "date-parts": [
      [
        2009,
        12
      ]
    ]
  }
}