Evidence map›Paper›PMID 11432824›Full record

ArticleThe EMBO journal2001

Lysine 188 substitutions convert the pattern of proteasome activation by REGgamma to that of REGs alpha and beta.

J Li, X Gao, J Ortega, T Nazif, L Joss, M Bogyo, A C Steven, M Rechsteiner

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. 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
  7. Article
  8. Article
  9. Proteome-wide modulation of degradation dynamics in response to growth arrest.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Proteasome allostery as a population shift between interchanging conformers.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  16. Article
  17. Article
  18. Proteasome activators.Molecular cell · 2011
    Review
  19. Review
  20. Article
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

8 authors at 1 institution in 1 country.

J LiDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132-0001, USA.
X Gao
J Ortega
T Nazif
L Joss
M Bogyo
A C Steven
M Rechsteiner
University of Utah · US

Funding

STRUCTURAL BIOLOGY OF MACROMOLECULAR COMPLEXESZ01AR027015 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI STEVEN, ALASDAIR C. · 1996 to 2008
$1.4M
MOLECULAR DISSECTION OF A PROTEASOME ACTIVATORR01GM060334 · NIGMS · UNIVERSITY OF UTAH · PI RECHSTEINER, MARTIN C · 2000 to 2003
$1.0M
NIGMS NIH HHS GM60334
6 · The paper itself

Abstract

11S REGs (PA28s) are multimeric rings that bind proteasomes and stimulate peptide hydrolysis. Whereas REGalpha activates proteasomal hydrolysis of peptides with hydrophobic, acidic or basic residues in the P1 position, REGgamma only activates cleavage after basic residues. We have isolated REGgamma mutants capable of activating the hydrolysis of fluorogenic peptides diagnostic for all three active proteasome beta subunits. The most robust REGgamma specificity mutants involve substitution of Glu or Asp for Lys188. REGgamma(K188E/D) variants are virtually identical to REGalpha in proteasome activation but assemble into less stable heptamers/hexamers. Based on the REGalpha crystal structure, Lys188 of REGgamma faces the aqueous channel through the heptamer, raising the possibility that REG channels function as substrate-selective gates. However, covalent modification of proteasome chymotrypsin-like subunits by 125I-YL3-VS demonstrates that REGgamma(K188E)'s activation of all three proteasome active sites is not due to relaxed gating. We propose that decreased stability of REGgamma(K188E) heptamers allows them to change conformation upon proteasome binding, thus relieving inhibition of the CT and PGPH sites normally imposed by the wild-type REGgamma molecule.

Indexed as

LysineNerve Tissue ProteinsAmino Acid SequenceAmino Acid SubstitutionAntigens, SurfaceAutoantigensCalcium-Binding ProteinsCrystallography, X-RayCysteine EndopeptidasesEnzyme ActivationLithostathineMacromolecular SubstancesMicroscopy, ElectronModels, MolecularMolecular Sequence DataMultienzyme ComplexesAntigens, SurfaceAutoantigensCalcium-Binding ProteinsCysteine EndopeptidasesKi antigenLithostathineLysineMacromolecular SubstancesMultienzyme ComplexesNerve Tissue ProteinsNuclear ProteinsPhosphoproteinsProteasome Endopeptidase ComplexProtein SubunitsRecombinant Proteins

Identifiers

PMID11432824
PMCPMC125523
OpenAlexW2150569981

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.