Evidence map›Paper›PMID 24103329›Full record

ArticleJournal of molecular biology2014

Multiple mechanisms for E2F binding inhibition by phosphorylation of the retinoblastoma protein C-terminal domain.

Jason R Burke, Tyler J Liban, Tamara Restrepo, Hsiau-Wei Lee, Seth M Rubin

Open access · bronzeAbstract read
In one paragraph

Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

31 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Chromatin association promotes UBR5-mediated degradation of Rb.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. The GScience advances · 2024
    Article
  5. Article
  6. The G1/S transition is promoted by Rb degradation via the E3 ligase UBR5.bioRxiv : the preprint server for biology · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Role of HPV16 E1 in cervical carcinogenesis.Frontiers in cellular and infection microbiology · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Detection of Retinoblastoma Protein Phosphorylation by Immunoblot Analysis.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  18. Article
  19. The Temporal Regulation of S Phase Proteins During GAdvances in experimental medicine and biology · 2017
    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

5 authors at 1 institution in 1 country.

Jason R BurkeDepartment of Chemistry and Biochemistry, University of California Santa Cruz, CA 95064, USA.
Tyler J LibanDepartment of Chemistry and Biochemistry, University of California Santa Cruz, CA 95064, USA.
Tamara RestrepoDepartment of Chemistry and Biochemistry, University of California Santa Cruz, CA 95064, USA.
Hsiau-Wei LeeDepartment of Chemistry and Biochemistry, University of California Santa Cruz, CA 95064, USA.
Seth M RubinDepartment of Chemistry and Biochemistry, University of California Santa Cruz, CA 95064, USA. Electronic address: srubin@ucsc.edu.
University of California, Santa Cruz · US

Funding

Molecular Mechanisms Regulating the Retinoblastoma Protein FamilyR01CA132685 · NCI · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI RUBIN, SETH MICHAEL · 2008 to 2017
$3.0M
NCI NIH HHS R01 CA132685
6 · The paper itself

Abstract

The retinoblastoma protein C-terminal domain (RbC) is necessary for the tumor suppressor protein's activities in growth suppression and E2F transcription factor inhibition. Cyclin-dependent kinase phosphorylation of RbC contributes to Rb inactivation and weakens the Rb-E2F inhibitory complex. Here we demonstrate two mechanisms for how RbC phosphorylation inhibits E2F binding. We find that phosphorylation of S788 and S795 weakens the direct association between the N-terminal portion of RbC (RbC(N)) and the marked-box domains of E2F and its heterodimerization partner DP. Phosphorylation of these sites and S807/S811 also induces an intramolecular association between RbC and the pocket domain, which overlaps with the site of E2F transactivation domain binding. A reduction in E2F binding affinity occurs with S788/S795 phosphorylation that is additive with the effects of phosphorylation at other sites, and we propose a structural mechanism that explains this additivity. We find that different Rb phosphorylation events have distinct effects on activating E2F family members, which suggests a novel mechanism for how Rb may differentially regulate E2F activities.

Indexed as

E2F Transcription FactorsHumansModels, BiologicalModels, MolecularPhosphorylationProtein BindingProtein ConformationRetinoblastoma ProteinE2F Transcription FactorsRetinoblastoma ProteinCDKcell cycle regulationcyclin-dependent kinasecyclin-dependent kinasesglutathione S-transferaseGSTheteronuclear single quantum coherenceHSQCisothermal titration calorimetryITCmultisite phosphorylationprotein–protein interactionsRb protein

Identifiers

PMID24103329
PMCPMC3872205
OpenAlexW2150203339

What OpenQuestion holds

Textmetadata
LicenceTDM
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.