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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9 May 2018

author

Hermann-Georg Holzhütter

6

object named as

Hermann-Georg Holzhütter

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Dawadschargal Bech-Otschir

1

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9 May 2018

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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9 May 2018

Nature Structural & Molecular Biology

published in

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9 May 2018

volume

16

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9 May 2018

issue

2

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9 May 2018

page(s)

219-225

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9 May 2018

https://scigraph.springernature.com/pub.10.1038/nsmb.1547

exact match

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cites work

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

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A cryptic protease couples deubiquitination and degradation by the proteasome

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

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

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

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A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal

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

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

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

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

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

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

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

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26S proteasome structure revealed by three-dimensional electron microscopy.

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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

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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

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Identifiers

DOI

10.1038/NSMB.1547

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9 May 2018

PubMed ID

19169257

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9 May 2018