Evidence map›Paper›PMID 18162577›Full record

ArticleMolecular biology of the cell2008

Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome.

Elena Koulich, Xiaohua Li, George N DeMartino

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed, 1 pooled it
6.4field-weighted citation impact, top 2% 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

132 citing papers in PubMed, 1 synthesis or guideline pooled it, 230 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Trial
  4. Review
  5. Article
  6. AKT and DUBs: a bidirectional relationship.Cellular & molecular biology letters · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  16. Article
  17. Ubiquitin-Specific Proteases (USPs) and Metabolic Disorders.International journal of molecular sciences · 2023
    Review
  18. Article
  19. Review
  20. Article

72 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

3 authors at 1 institution in 1 country.

Elena KoulichDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9040, USA.
Xiaohua Li
George N DeMartino
The University of Texas Southwestern Medical Center · US

Funding

FUNCTION AND REGULATION OF THE PROTEASOMER01DK046181 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI DEMARTINO, GEORGE N. · 1994 to 2012
$3.2M
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 R01 DK046181NIDDK NIH HHS R56 DK046181
6 · The paper itself

Abstract

We determined composition and relative roles of deubiquitylating proteins associated with the 26S proteasome in mammalian cells. Three deubiquitylating activities were associated with the 26S proteasome: two from constituent subunits, Rpn11/S13 and Uch37, and one from a reversibly associated protein, Usp14. RNA interference (RNAi) of Rpn11/S13 inhibited cell growth, decreased cellular proteasome activity via disrupted 26S proteasome assembly, and inhibited cellular protein degradation. In contrast, RNAi of Uch37 or Usp14 had no detectable effect on cell growth, proteasome structure or proteolytic capacity, but accelerated cellular protein degradation. RNAi of both Uch37 and Usp14 also had no effect on proteasome structure or proteolytic capacity, but inhibited cellular protein degradation. Thus, proper proteasomal processing of ubiquitylated substrates requires Rpn11 plus either Uch37 or Usp14. Although the latter proteins feature redundant deubiquitylation functions, they also appear to exert noncatalyic effects on proteasome activity that are similar to but independent of one another. These results reveal unexpected functional relationships among multiple deubiquitylating proteins and suggest a model for mammalian 26S proteasome function whereby their concerted action governs proteasome function by linking deubiquitylation to substrate hydrolysis.

Indexed as

AnimalsCattleCell ExtractsEndopeptidasesHeLa CellsHumansProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalRNA InterferenceSodium ChlorideStructure-Activity RelationshipUbiquitinationATP dependent 26S proteaseCell ExtractsEndopeptidasesProteasome Endopeptidase ComplexSodium Chloride

Identifiers

PMID18162577
PMCPMC2262970
OpenAlexW2099857411

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.