Evidence map›Paper›PMID 22992741›Full record

ArticleThe Journal of biological chemistry2012

The archaeal proteasome is regulated by a network of AAA ATPases.

Dara Forouzan, Moritz Ammelburg, Cedric F Hobel, Luisa J Ströh, Nicole Sessler, Jörg Martin, Andrei N Lupas

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 49 citations in OpenAlex.

  1. Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Probing allosteric interactions in homo-oligomeric molecular machines using solution NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Exploring long-range cooperativity in the 20S proteasome core particle fromProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Stepping up protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Probing the cooperativity ofProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Article
  17. Review
  18. Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Article
  20. Review
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

7 authors at 2 institutions in 1 country.

Dara ForouzanDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, D-72076 Tübingen, Germany.
Moritz Ammelburg
Cedric F Hobel
Luisa J Ströh
Nicole Sessler
Jörg Martin
Andrei N Lupas
Max Planck Institute for Developmental Biology · DEUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteasome is the central machinery for targeted protein degradation in archaea, Actinobacteria, and eukaryotes. In its basic form, it consists of a regulatory ATPase complex and a proteolytic core particle. The interaction between the two is governed by an HbYX motif (where Hb is a hydrophobic residue, Y is tyrosine, and X is any amino acid) at the C terminus of the ATPase subunits, which stimulates gate opening of the proteasomal α-subunits. In archaea, the proteasome-interacting motif is not only found in canonical proteasome-activating nucleotidases of the PAN/ARC/Rpt group, which are absent in major archaeal lineages, but also in proteins of the CDC48/p97/VAT and AMA groups, suggesting a regulatory network of proteasomal ATPases. Indeed, Thermoplasma acidophilum, which lacks PAN, encodes one CDC48 protein that interacts with the 20S proteasome and activates the degradation of model substrates. In contrast, Methanosarcina mazei contains seven AAA proteins, five of which, both PAN proteins, two out of three CDC48 proteins, and the AMA protein, function as proteasomal gatekeepers. The prevalent presence of multiple, distinct proteasomal ATPases in archaea thus results in a network of regulatory ATPases that may widen the substrate spectrum of proteasomal protein degradation.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceArchaeaArchaeal ProteinsCell Cycle ProteinsChromatography, LiquidCloning, MolecularComputational BiologyGene Expression Regulation, ArchaealMass SpectrometryMethanosarcinaModels, BiologicalMolecular Sequence DataPhylogenyProteasome Endopeptidase ComplexSubstrate SpecificityAdenosine TriphosphatasesArchaeal ProteinsCell Cycle ProteinsPAN enzymeProteasome Endopeptidase ComplexValosin Containing Protein

Identifiers

PMID22992741
PMCPMC3493965
OpenAlexW2071746920

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.