ArticleJournal of molecular biology2016
Structural Conservation and E2F Binding Specificity within the Retinoblastoma Pocket Protein Family.
Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Review
- Chromatin association promotes UBR5-mediated degradation of Rb.bioRxiv : the preprint server for biology · 2026Article
- The E2F family: a ray of dawn in cardiomyopathy.Molecular and cellular biochemistry · 2025Review
- Review
- Identification and validation of a novel long non-coding RNA (LINC01465) in ovarian cancer.Human cell · 2023Review
- Structural basis for tunable affinity and specificity of LxCxE-dependent protein interactions with the retinoblastoma protein family.Structure (London, England : 1993) · 2022Article
- Structure of a nucleosome-bound MuvB transcription factor complex reveals DNA remodelling.Nature communications · 2022Article
- Article
- Structure and function of MuvB complexes.Oncogene · 2022Review
- Early 2 factor (E2F) transcription factors contribute to malignant progression and have clinical prognostic value in lower-grade glioma.Bioengineered · 2021Article
- The Role and Clinical Implications of the Retinoblastoma (RB)-E2F Pathway in Gastric Cancer.Frontiers in oncology · 2021Review
- Transcriptional E2F1/2/3/6 as potential prognostic biomarkers in cutaneous melanoma.American journal of translational research · 2021Article
- Article
- DREAM and RB cooperate to induce gene repression and cell-cycle arrest in response to p53 activation.Nucleic acids research · 2019Article
- E2F4 regulates transcriptional activation in mouse embryonic stem cells independently of the RB family.Nature communications · 2019Article
- The broken cycle: E2F dysfunction in cancer.Nature reviews. Cancer · 2019Review
- The miR-181 family promotes cell cycle by targeting CTDSPL, a phosphatase-like tumor suppressor in uveal melanoma.Journal of experimental & clinical cancer research : CR · 2018Article
- Conservation and divergence of C-terminal domain structure in the retinoblastoma protein family.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Human cytomegalovirus-encoded viral cyclin-dependent kinase (v-CDK) UL97 phosphorylates and inactivates the retinoblastoma protein-related p107 and p130 proteins.The Journal of biological chemistry · 2017Article
- MicroRNA-1179 inhibits glioblastoma cell proliferation and cell cycle progression via directly targeting E2F transcription factor 5.American journal of cancer research · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The human pocket proteins retinoblastoma (Rb), p107, and p130 are critical negative regulators of the cell cycle and contribute to tumor suppression. While strong structural conservation within the pocket protein family provides for some functional redundancy, important differences have been observed and may underlie the reason that Rb is a uniquely potent tumor suppressor. It has been proposed that distinct pocket protein activities are mediated by their different E2F transcription factor binding partners. In humans, Rb binds E2F1-E2F5, whereas p107 and p130 almost exclusively associate with E2F4 and E2F5. To identify the molecular determinants of this specificity, we compared the crystal structures of Rb and p107 pocket domains and identified several key residues that contribute to E2F selectivity in the pocket family. Mutation of these residues in p107 to match the analogous residue in Rb results in an increase in affinity for E2F1 and E2F2 and an increase in the ability of p107 to inhibit E2F2 transactivation. Additionally, we investigated how phosphorylation by Cyclin-dependent kinase on distinct residues regulates p107 affinity for the E2F4 transactivation domain. We found that phosphorylation of residues S650 and S975 weakens the E2F4 transactivation domain binding. Our data reveal molecular features of pocket proteins that are responsible for their similarities and differences in function and regulation.
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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.