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TRF2 deficiency led to a 1,5-2 fold increase in the radiosensitivity of hMSC-telo1 (show ATM Proteins) 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 Proteins) is down-regulated in the TRF2(DeltaBDeltaM)-induced senescence, which was mediated by ATM (show ATM Proteins) and p38 MAPK (show MAPK14 Proteins)
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 Proteins) and TRF2
that a dimer of the shelterin subunit TRF2 wraps approximately 90 bp of DNA through several lysine and arginine residues localized around its homodimerization domain.
TRF2 overexpression results in replication stalling in duplex telomeric repeat tracts and formation of telomeric ultrafine anaphase bridges, ultimately leading to stochastic loss of telomeric sequences.
APB (show RNPEP Proteins) formation induced clustering of telomere repeats, telomere compaction and concomitant depletion of the shelterin protein TRF2 (also known as TERF2).
Study demonstrates that TRF2 interacts with and is sumoylated by PIAS1 (show PIAS1 Proteins) and RNF4 (show RNF4 Proteins) targets SUMO-conjugated TRF2 for ubiquitination, thereby decreasing its stability suggesting that TRF2 status provides a molecular switch that controls its level at telomeres.
Overexpressing TRF2-S and silencing FMRP (show FMR1 Proteins) 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 Proteins) platelet-derived growth factor receptor beta (show PDGFRB Proteins) (PDGFRbeta).
role of TRF2 in skin homeostasis, is reported.
shelterin protein TIN2 (show TINF2 Proteins) can protect chromosome ends as a TRF2-tethered TIN2 (show TINF2 Proteins)/TPP1 (show TPP1 Proteins)/POT1 (show POT1 Proteins) complex that lacks a physical connection to TRF1 (show TERF1 Proteins)
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 Proteins), Rap1 (show TERF2IP Proteins), or the POT1 (show POT1 Proteins) proteins (POT1a (show POT1 Proteins) and POT1b) had no effect on the frequency of t-loop occurrence.
TAF7L (show TAF7L Proteins) associates with TRF2 both in vitro and in testis, suggesting that TAF7L (show TAF7L Proteins) 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 Proteins) controls the ubiquitin-proteasome system in VSMC & regulates doxorubicin-induced TRF2 ubiquitination and proteasomal degradation via this mechanism.
the molecular properties of TRF2 that are both necessary and sufficient to protect chromosome ends in mouse embryonic fibroblasts: the data support a two-step mechanism for TRF2-mediated end protection
TRF2 provides a crucial link between telomere function and ultraviolet-induced damage repair, whose alteration underlies genomic instability, cancer and aging.
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