Evidence map›Paper›PMID 17018291›Full record

ArticleMolecular cell2006

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

Chang-Wei Liu, Xiaohua Li, David Thompson, Kerry Wooding, Tsui-ling Chang, Zhanyun Tang, Hongtao Yu, Philip J Thomas, George N DeMartino

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed, 1 pooled it
5.6field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

113 citing papers in PubMed, 1 synthesis or guideline pooled it, 187 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. The Time-Resolved Salt Stress Response ofInternational journal of molecular sciences · 2023
    Article
  9. The ATP-dependent Pathways and Human Diseases.Current medicinal chemistry · 2023
    Article
  10. Article
  11. Article
  12. Early Forms ofBiomolecules · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Proteins containing ubiquitin-like (Ubl) domains not only bind to 26S proteasomes but also induce their activation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. Article

53 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Chang-Wei LiuDepartment of Physiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
Xiaohua Li
David Thompson
Kerry Wooding
Tsui-ling Chang
Zhanyun Tang
Hongtao Yu
Philip J Thomas
George N DeMartino
The University of Texas Southwestern Medical Center · US

Funding

DEVELOPMENT OF MEMBRANE PROTEIN STRUCTURER37DK049835 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI THOMAS, PHILIP J · 2008 to 2017
$3.6M
FUNCTION AND REGULATION OF THE PROTEASOMER01DK046181 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI DEMARTINO, GEORGE N. · 1994 to 2012
$3.2M
Development of Membrane Protein StructureR01DK049835 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI THOMAS, PHILIP J · 1996 to 2007
$2.1M
Function and regulation of the proteasomeR56DK046181 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI DEMARTINO, GEORGE N. · 2007 to 2007
$353k
NIDDK NIH HHS DK 46181NIDDK NIH HHS DK 49835NIDDK NIH HHS R01 DK046181NIDDK NIH HHS R01 DK049835NIDDK NIH HHS R37 DK049835NIDDK NIH HHS R56 DK046181
6 · The paper itself

Abstract

The 26S proteasome degrades polyubiquitinated proteins by an energy-dependent mechanism. Here we define multiple roles for ATP in 26S proteasome function. ATP binding is necessary and sufficient for assembly of 26S proteasome from 20S proteasome and PA700/19S subcomplexes and for proteasome activation. Proteasome assembly and activation may require distinct ATP binding events. The 26S proteasome degrades nonubiquitylated, unstructured proteins without ATP hydrolysis, indicating that substrate translocation per se does not require the energy of hydrolysis. Nonubiquitylated folded proteins and certain polyubiquitylated folded proteins were refractory to proteolysis. The latter were deubiquitylated by an ATP-independent mechanism. Other folded as well as unstructured polyubiquitylated proteins required ATP hydrolysis for proteolysis and deubiquitylation. Thus, ATP hydrolysis is not used solely for substrate unfolding. These results indicate that 26S proteasome-catalyzed degradation of polyubiquitylated proteins involves mechanistic coupling of several processes and that such coupling imposes an energy requirement not apparent for any isolated process.

Indexed as

Adenosine TriphosphateAnimalsCattleEnzyme StabilityHumansHydrolysisModels, BiologicalProteasome Endopeptidase ComplexProtein FoldingUbiquitinAdenosine TriphosphateATP dependent 26S proteasePA700 proteasome activatorProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID17018291
PMCPMC3951175
OpenAlexW2116724545

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.