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our findings describe TRF2 as a novel SIRT6 (show SIRT6 ELISA Kits) substrate and demonstrate that acetylation of TRF2 plays a crucial role in the regulation of TRF2 protein stability, thus providing a new route for modulating its expression level during oncogenesis and damage response.
The results suggest that dimerized TRF2 recruits origin recognition complex and stimulates pre-replication complex formation at telomeres through the TRFH domain.
Studied the disruption pattern of of 3D telomere-TRF2 interaction in the progression from mononuclear Hodgkin cells (H) to multinucleated Reed-Sternberg cells (RS).
TRF2, a component of shelterin, binds to core histones to protect chromosome ends from inappropriate DNA damage response and loss of telomeric DNA. The N-terminal Gly/Arg-rich domain (GAR domain) of TRF2 directly binds to the globular domain of core histones.
TRF2 deficiency led to a 1,5-2 fold increase in the radiosensitivity of hMSC-telo1 (show ATM ELISA Kits) cells through telomere destabilization.
DREEM imaging shows that in contrast to chromatin with DNA wrapping around histones, large TRF2-DNA complexes (with volumes larger than TRF2 tetramers) compact DNA inside TRF2 with portions of folded DNA appearing at the edge of these complexes.
observed that the expression of Sp1 (show PSG1 ELISA Kits) is down-regulated in the TRF2(DeltaBDeltaM)-induced senescence, which was mediated by ATM (show ATM ELISA Kits) and p38 MAPK (show MAPK14 ELISA Kits)
Data show that isoform beta2 of the heregulin (HRGbeta2) localizes at telomeres with the telomere-associated proteins TRF2 and RAP1.
These observations suggest that TRF2 is a good candidate for the attachment of telomeres to the nuclear envelope in somatic cells
Through a combination of biochemical, biophysical and structural approaches, we unveiled a unique mode of assembly between RAP1 (show RABGEF1 ELISA Kits) and TRF2
The authors propose that TRF2 masks and stabilizes the t-loop three-way junction, thereby protecting telomeres from detrimental deletions and PARP1 (show PARP1 ELISA Kits) activation.
Overexpressing TRF2-S and silencing FMRP (show FMR1 ELISA Kits) promotes mRNA entry to axons and enhances axonal outgrowth and neurotransmitter release from presynaptic terminals.
TRF2 binds and transactivates the promoter of the angiogenic tyrosine kinase (show TYRO3 ELISA Kits) platelet-derived growth factor receptor beta (show PDGFRB ELISA Kits) (PDGFRbeta).
role of TRF2 in skin homeostasis, is reported.
shelterin protein TIN2 (show TINF2 ELISA Kits) can protect chromosome ends as a TRF2-tethered TIN2 (show TINF2 ELISA Kits)/TPP1 (show TPP1 ELISA Kits)/POT1 (show POT1 ELISA Kits) complex that lacks a physical connection to TRF1 (show TERF1 ELISA Kits)
We concluded that genomic instability resulting from loss of TRF2 expression provides biological advantages to the cancer stem cell population
Conditional deletion of individual components of shelterin showed that TRF2 was required for the formation and/or maintenance of t-loops, whereas deletion of TRF1 (show TERF1 ELISA Kits), Rap1 (show TERF2IP ELISA Kits), or the POT1 (show POT1 ELISA Kits) proteins (POT1a (show POT1 ELISA Kits) and POT1b) had no effect on the frequency of t-loop occurrence.
TAF7L (show TAF7L ELISA Kits) associates with TRF2 both in vitro and in testis, suggesting that TAF7L (show TAF7L ELISA Kits) likely cooperates directly with TRF2 at promoters of a subset of postmeiotic genes to regulate spermiogenesis.
Experiments in cells from knockout mice showed that uPAR (show PLAUR ELISA Kits) controls the ubiquitin-proteasome system in VSMC & regulates doxorubicin-induced TRF2 ubiquitination and proteasomal degradation via this mechanism.
This gene encodes a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. This protein is present at telomeres in metaphase of the cell cycle, is a second negative regulator of telomere length and plays a key role in the protective activity of telomeres. While having similar telomere binding activity and domain organization, TERF2 differs from TERF1 in that its N terminus is basic rather than acidic.
telomeric repeat binding factor 2
, TTAGGG repeat-binding factor 2
, telomeric DNA-binding protein
, telomeric repeat binding protein 2
, telomeric repeat-binding factor 2
, TTAGGG-repeat binding factor 2 TRF2
, telomeric repeat binding factor a
, TTAGGG repeat binding factor 2