Evidence map›Paper›PMID 20717473›Full record

ArticleFrontiers in molecular neuroscience2010

Characterization of the Brain 26S Proteasome and its Interacting Proteins.

Hwan-Ching Tai, Henrike Besche, Alfred L Goldberg, Erin M Schuman

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular neuroscience, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

93 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
  2. PI31 expression is neuroprotective in a mouse model of early-onset parkinsonism.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. More 26S and 30S proteasomes are beneficial in proteinopathy.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Proteasome localization and activity in pig brain andFrontiers in cellular neuroscience · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Activity-Induced Cortical Glutamatergic Neuron Nascent Proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Protein Aggregation in the Pathogenesis of Ischemic Stroke.Cellular and molecular neurobiology · 2021
    Review
  19. Article
  20. Article

33 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

4 authors at 1 institution in 1 country.

Hwan-Ching TaiDivision of Chemistry and Chemical Engineering, California Institute of Technology Pasadena, CA, USA.
Henrike Besche
Alfred L Goldberg
Erin M Schuman
California Institute of Technology · US

Funding

MOLECULAR CHAPERONES AND PROTEIN DEGRADATIONR01GM051923 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLDBERG, ALFRED L · 1995 to 2020
$10.1M
NIGMS NIH HHS R01 GM051923
6 · The paper itself

Abstract

Proteasome-mediated proteolysis is important for synaptic plasticity, neuronal development, protein quality control, and many other processes in neurons. To define proteasome composition in brain, we affinity purified 26S proteasomes from cytosolic and synaptic compartments of the rat cortex. Using tandem mass spectrometry, we identified the standard 26S subunits and a set of 28 proteasome-interacting proteins that associated substoichiometrically and may serve as regulators or cofactors. This set differed from those in other tissues and we also found several proteins that associated only with either the cytosolic or the synaptic proteasome. The latter included the ubiquitin-binding factor TAX1BP1 and synaptic vesicle protein SNAP-25. Native gel electrophoresis revealed a higher proportion of doubly-capped 26S proteasome (19S-20S-19S) in the cortex than in the liver or kidney. To investigate the interplay between proteasome regulation and synaptic plasticity, we exposed cultured neurons to glutamate receptor agonist NMDA. Within 4 h, this agent caused a prolonged decrease in the activity of the ubiquitin-proteasome system as shown by disassembly of 26S proteasomes, decrease in ubiquitin-protein conjugates, and dissociation of the ubiquitin ligases UBE3A (E6-AP) and HUWE1 from the proteasome. Surprisingly, the regulatory 19S particles were rapidly degraded by proteasomal, not lysosomal degradation, and the dissociated E3 enzymes also degraded. Thus the content of proteasomes and their set of associated proteins can be altered by neuronal activity, in a manner likely to influence synaptic plasticity and learning.

Indexed as

NMDAproteasomeproteasome-interacting proteinsynaptic plasticityUBE3Aubiquitin ligase

Identifiers

PMID20717473
PMCPMC2901091
OpenAlexW2018228226

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.