Evidence map›Paper›PMID 32332747›Full record

ArticleNature communications2020

A masked initiation region in retinoblastoma protein regulates its proteasomal degradation.

Takuya Tomita, Jon M Huibregtse, Andreas Matouschek

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. 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
2.0field-weighted citation impact, top 13% 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, 41 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Nutrition research and practice · 2025
    Article
  9. The GScience advances · 2024
    Article
  10. The G1/S transition is promoted by Rb degradation via the E3 ligase UBR5.bioRxiv : the preprint server for biology · 2024
    Article
  11. Calpain and Cardiometabolic Diseases.International journal of molecular sciences · 2023
    Review
  12. TheBiomedicines · 2023
    Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Site-specific ubiquitination: Deconstructing the degradation tag.Current opinion in structural biology · 2022
    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

3 authors at 1 institution in 1 country.

Takuya TomitaDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, 78712, USA.ORCID http://orcid.org/0000-0003-4568-9940
Jon M HuibregtseDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, 78712, USA.
Andreas MatouschekDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, 78712, USA. matouschek@austin.utexas.edu.ORCID http://orcid.org/0000-0001-6016-2341
The University of Texas at Austin · US

Funding

TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI WIDOM, JONATHAN · 2009 to 2013
$12.8M
Deciphering a second component to the proteasomal degradation codeR01GM124501 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MATOUSCHEK, ANDREAS · 2017 to 2020
$1.6M
Development of proteasome adaptors to catalytically deplete specific proteins from cellsR21CA196456 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI MATOUSCHEK, ANDREAS · 2016 to 2018
$597k
NCI NIH HHS R21 CA196456NCI NIH HHS U54 CA143869NIGMS NIH HHS R01 GM124501
6 · The paper itself

Abstract

Retinoblastoma protein (Rb) is a tumor suppressor that binds and represses E2F transcription factors. In cervical cancer cells, human papilloma virus (HPV) protein E7 binds to Rb, releasing it from E2F to promote cell cycle progression, and inducing ubiquitination of Rb. E7-mediated proteasomal degradation of Rb requires action by another protease, calpain, which cleaves Rb after Lys 810. However, it is not clear why cleavage is required for Rb degradation. Here, we report that the proteasome cannot initiate degradation efficiently on full-length Rb. Calpain cleavage exposes a region that is recognized by the proteasome, leading to rapid proteolysis of Rb. These findings identify a mechanism for regulating protein stability by controlling initiation and provide a better understanding of the molecular mechanism underlying transformation by HPV.

Indexed as

Gene Expression Regulation, NeoplasticAcrylatesCalpainCell CycleCell Transformation, NeoplasticCyclopentanesE2F Transcription FactorsFemaleHEK293 CellsHuman papillomavirus 16HumansNEDD8 ProteinOligopeptidesPapillomavirus E7 ProteinsProteasome Endopeptidase ComplexProtein StabilityAcrylatesCalpainCAPN1 protein, humancarfilzomibCyclopentanesE2F Transcription FactorsNEDD8 ProteinNEDD8 protein, humanOligopeptidesoncogene protein E7, Human papillomavirus type 16Papillomavirus E7 ProteinsPD 150606pevonedistatProteasome Endopeptidase ComplexPyrimidinesRB1 protein, humanRecombinant ProteinsRetinoblastoma Binding ProteinsUbiquitin-Protein Ligases

Identifiers

PMID32332747
PMCPMC7181824
OpenAlexW3020625982

What OpenQuestion holds

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LicenceCC BY
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.