Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome. (Q52913169)

9 May 2018

title

Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome. (English)

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author

Hermann-Georg Holzhütter

6

object named as

Hermann-Georg Holzhütter

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author name string

Dawadschargal Bech-Otschir

1

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Annett Helfrich

2

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Cordula Enenkel

3

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Gesa Consiglieri

4

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Michael Seeger

5

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Burkhardt Dahlmann

7

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Peter-Michael Kloetzel

8

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publication date

25 January 2009

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Nature Structural & Molecular Biology

published in

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9 May 2018

volume

16

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issue

2

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page(s)

219-225

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Studies on the activation by ATP of the 26 S proteasome complex from rat skeletal muscle

cites work

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The 26S proteasome: a molecular machine designed for controlled proteolysis

21 January 2018

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A gated channel into the proteasome core particle

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Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors

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ATP binding and ATP hydrolysis play distinct roles in the function of 26S proteasome

31 March 2020

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Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome

31 March 2020

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A cryptic protease couples deubiquitination and degradation by the proteasome

31 March 2020

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Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome

31 March 2020

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The base of the proteasome regulatory particle exhibits chaperone-like activity

31 March 2020

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The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release

31 March 2020

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Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry

31 March 2020

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A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal

31 March 2020

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Proteasomes and their kin: proteases in the machine age

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HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation

31 March 2020

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Regulatory subunit interactions of the 26S proteasome, a complex problem

31 March 2020

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ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle

31 March 2020

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Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites.

31 March 2020

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The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1

31 March 2020

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Recognition of the polyubiquitin proteolytic signal

31 March 2020

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Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin

31 March 2020

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Evidence for the existence of a non-catalytic modifier site of peptide hydrolysis by the 20 S proteasome

31 March 2020

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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

31 March 2020

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Getting in and out of the proteasome

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The substrate translocation channel of the proteasome

31 March 2020

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Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system

31 March 2020

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ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation

31 March 2020

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Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome

31 March 2020

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Mechanism and function of deubiquitinating enzymes

31 March 2020

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Kinetic evidences for facilitation of peptide channelling by the proteasome activator PA28.

31 March 2020

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Reconstitution of hybrid proteasomes from purified PA700-20 S complexes and PA28alphabeta activator: ultrastructure and peptidase activities

31 March 2020

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26S proteasome structure revealed by three-dimensional electron microscopy

31 March 2020

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Structure of the human 26S proteasome: subunit radial displacements open the gate into the proteolytic core

31 March 2020

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The interferon-gamma-inducible 11 S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20 S proteasome in vitro

31 March 2020

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The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin alphabeta and proteasome functions

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSMB.1547

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9 May 2018

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9 May 2018