Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Pocket proteins and cell cycle control.

David Cobrinik1

  • 1Dyson Vision Research Institute and Department of Ophthalmology, Weill Medical College of Cornell University, 1300 York Avenue, LC303, New York, NY 10021, USA. dec2014@med.cornell.edu

Oncogene
|April 20, 2005
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Expression of HER2 in the eye and the potential for on-target side effects with antibody-drug conjugates.

Scientific reports·2026
Same author

Trio exome sequencing of an optic nerve hypoplasia cohort reveals evidence for polygenic architecture.

Ophthalmic genetics·2025
Same author

Identification and characterization of early human photoreceptor states and cell-state-specific retinoblastoma-related features.

eLife·2025
Same author

Chevreul: an R bioconductor package for exploratory analysis of full-length single cell sequencing.

GigaByte (Hong Kong, China)·2025
Same author

Chevreul: An R Bioconductor Package for Exploratory Analysis of Full-Length Single Cell Sequencing.

bioRxiv : the preprint server for biology·2025
Same author

Phenotypic Biomarkers of Aqueous Extracellular Vesicles from Retinoblastoma Eyes.

International journal of molecular sciences·2024
Same journal

SRD5A3-mediated aberrant N-glycosylation of SCARA5 promotes ferroptosis in lung adenocarcinoma.

Oncogene·2026
Same journal

Aberrant splicing in human cancer shows possible functional impact on transcription factors.

Oncogene·2026
Same journal

The crosstalk between RNA m6A modification and protein lactylation: emerging insights into tumor progression.

Oncogene·2026
Same journal

Correction: Neuropilin-1 promotes human glioma progression through potentiating the activity of the HGF/SF autocrine pathway.

Oncogene·2026
Same journal

Amphiregulin-mediated EGFR activation drives both intrinsic and acquired resistance to KRAS G12C inhibitors in KRAS G12C-mutant non-small cell lung cancer.

Oncogene·2026
Same journal

Histone lactylation-driven IGF2BP3 promotes intrahepatic cholangiocarcinoma progression via SPP1/CD44-dependent macrophage polarization.

Oncogene·2026
See all related articles

The pocket protein family, including retinoblastoma protein (pRB), p107, and p130, regulates the cell cycle by controlling gene expression and cell transitions. Further research is needed to fully understand their developmental and tumor suppressor roles.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The pocket protein family (pRB, p107, p130) are key regulators of the cell cycle.
  • They primarily restrain the G1-S transition by managing E2F-responsive genes.
  • These proteins also play roles in senescence, differentiation, and E2F-independent cell cycle control.

Purpose of the Study:

  • To review and synthesize current knowledge on pocket protein function and regulation.
  • To highlight recent advances in understanding pocket protein mechanisms.
  • To identify areas requiring further investigation, particularly regarding developmental and tumor suppressor functions.

Main Methods:

  • Literature review and synthesis of existing research on pocket proteins.
  • Analysis of studies on gene regulation, cell cycle transitions, and protein interactions.

Related Experiment Videos

  • Examination of recent findings on pocket protein phosphorylation and dephosphorylation.
  • Main Results:

    • Pocket proteins regulate distinct gene sets through selective E2F interactions.
    • They contribute to gene silencing during senescence and differentiation.
    • New insights reveal redundancy in previously identified kinases and novel phosphorylation/dephosphorylation mechanisms.

    Conclusions:

    • Pocket proteins are crucial for cell cycle control, exhibiting both E2F-dependent and independent functions.
    • Recent discoveries have refined our understanding of their regulatory mechanisms.
    • Further research is essential to elucidate their complex roles in development and tumor suppression.