ArticleThe Journal of biological chemistry2012
Human Rap1 interacts directly with telomeric DNA and regulates TRF2 localization at the telomere.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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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.
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Who cites it
43 citing papers in PubMed, 57 citations in OpenAlex.
- Telomere-associated non-malignant pulmonary diseases: Pathogenic mechanisms and therapeutic strategies.Acta pharmaceutica Sinica. B · 2026Review
- Telomere-related DNA damage response pathways in cancer therapy: prospective targets.Frontiers in pharmacology · 2024Review
- Rap1 regulates TIP60 function during fate transition between two-cell-like and pluripotent states.Genes & development · 2022Article
- TIN2 is an architectural protein that facilitates TRF2-mediated trans- and cis-interactions on telomeric DNA.Nucleic acids research · 2021Article
- Review
- The Intra- and Extra-Telomeric Role of TRF2 in the DNA Damage Response.International journal of molecular sciences · 2021Review
- Review
- Aging and Protein Kinases.Advances in experimental medicine and biology · 2021Article
- Nuclear Accumulation of LAP1:TRF2 Complex during DNA Damage Response Uncovers a Novel Role for LAP1.Cells · 2020Article
- Role of Telomeres and Telomeric Proteins in Human Malignancies and Their Therapeutic Potential.Cancers · 2020Review
- Therapeutic Targets in Telomerase and Telomere Biology of Cancers.Indian journal of clinical biochemistry : IJCB · 2020Review
- A Global Screen for Assembly State Changes of the Mitotic Proteome by SEC-SWATH-MS.Cell systems · 2020Article
- Either Rap1 or Cdc13 can protect telomeric single-stranded 3' overhangs from degradation in vitro.Scientific reports · 2019Article
- Rap1 regulates hematopoietic stem cell survival and affects oncogenesis and response to chemotherapy.Nature communications · 2019Article
- Review
- Telomeres: Implications for Cancer Development.International journal of molecular sciences · 2018Review
- Dissecting the telomere-inner nuclear membrane interface formed in meiosis.Nature structural & molecular biology · 2017Article
- Reconstitution of human shelterin complexes reveals unexpected stoichiometry and dual pathways to enhance telomerase processivity.Nature communications · 2017Article
- Rap1 and Cdc13 have complementary roles in preventing exonucleolytic degradation of telomere 5' ends.Scientific reports · 2017Article
- PRL-3 promotes telomere deprotection and chromosomal instability.Nucleic acids research · 2017Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The TRF2-Rap1 complex suppresses non-homologous end joining and interacts with DNAPK-C to prevent end joining. We previously demonstrated that hTRF2 is a double strand telomere binding protein that forms t-loops in vitro and recognizes three- and four-way junctions independent of DNA sequence. How the DNA binding characteristics of hTRF2 to DNA is altered in the presence of hRap1 however is not known. Here we utilized EM and quantitative gel retardation to characterize the DNA binding properties of hRap1 and the TRF2-Rap1 complex. Both gel filtration chromatography and mass analysis from two-dimensional projections showed that the TRF2-Rap1 complex exists in solution and binds to DNA as a complex consisting of four monomers each of hRap1 and hTRF2. EM revealed for the first time that hRap1 binds to DNA templates in the absence of hTRF2 with a preference for double strand-single strand junctions in a sequence independent manner. When hTRF2 and hRap1 are in a complex, its affinity for ds telomeric sequences is 2-fold higher than TRF2 alone and more than 10-fold higher for telomeric 3' ends. This suggests that as hTRF2 recruits hRap1 to telomeric sequences, hRap1 alters the affinity of hTRF2 and its binding preference on telomeric DNA. Moreover, the TRF2-Rap1 complex has higher ability to re-model telomeric DNA than either component alone. This finding underlies the importance of complex formation between hRap1 and hTRF2 for telomere function and end protection.
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Registered trials
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.