Evidence map›Paper›PMID 11248031›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit.

Y Xie, A Varshavsky

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 226 papers.

0numbers the graph read from it
0cells of the map it votes in
226citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

226 citing papers in PubMed, 449 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Mechanism of autocatalytic activation during proteasome assembly.Nature structural & molecular biology · 2024
    Article
  17. Article
  18. Article
  19. Proteotoxic stress and the ubiquitin proteasome system.Seminars in cell & developmental biology · 2024
    Review
  20. Article

166 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

2 authors at 1 institution in 1 country.

Y XieDivision of Biology, California Institute of Technology, Pasadena, CA 91125, USA.
A Varshavsky
California Institute of Technology · US

Funding

The Functions, Mechanisms, and Regulation of N-Terminal ArginylationR01GM031530 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALEXANDER J VARSHAVSKY · 1985 to 2026
$14.5M
Ubiquitin Ligases, Mechanisms and Functions of the N-End Rule PathwayR01DK039520 · NIDDK · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI VARSHAVSKY, ALEXANDER J · 1988 to 2025
$10.0M
MECHANICS AND FUNCTIONS OF THE N-END RULE PATHWAYR37DK039520 · NIDDK · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI VARSHAVSKY, ALEXANDER J · 1998 to 2007
$4.4M
Ubiquitin Ligases, Mechanisms and Functions of the N-End Rule PathwayR56DK039520 · NIDDK · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI VARSHAVSKY, ALEXANDER J · 2008 to 2008
$161k
NIDDK NIH HHS DK39520NIDDK NIH HHS R01 DK039520NIDDK NIH HHS R37 DK039520NIDDK NIH HHS R56 DK039520NIGMS NIH HHS GM31530NIGMS NIH HHS R01 GM031530
6 · The paper itself

Abstract

The RPN4 (SON1, UFD5) protein of the yeast Saccharomyces cerevisiae is required for normal levels of intracellular proteolysis. RPN4 is a transcriptional activator of genes encoding proteasomal subunits. Here we show that RPN4 is required for normal levels of these subunits. Further, we demonstrate that RPN4 is extremely short-lived (t(1/2) approximately 2 min), that it directly interacts with RPN2, a subunit of the 26S proteasome, and that rpn4Delta cells are perturbed in their cell cycle. The degradation signal of RPN4 was mapped to its N-terminal region, outside the transcription-activation domains of RPN4. The ability of RPN4 to augment the synthesis of proteasomal subunits while being metabolically unstable yields a negative feedback circuit in which the same protein up-regulates the proteasome production and is destroyed by the assembled active proteasome.

Indexed as

Saccharomyces cerevisiae ProteinsBinding SitesCell DivisionCysteine EndopeptidasesDNA-Binding ProteinsFungal ProteinsG1 PhaseGene Expression RegulationLigandsMultienzyme ComplexesPeptide HydrolasesProteasome Endopeptidase ComplexRibonucleoproteinsRibosomal ProteinsRNA-Binding ProteinsSaccharomyces cerevisiaeATP dependent 26S proteaseCysteine EndopeptidasesDNA-Binding ProteinsFungal ProteinsLigandsMultienzyme ComplexesPeptide HydrolasesProteasome Endopeptidase ComplexRibonucleoproteinsRibosomal ProteinsRNA-Binding ProteinsRNP1 protein, S cerevisiaeRPN4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitin

Identifiers

PMID11248031
PMCPMC30606
OpenAlexW2112660386

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.