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ROC curves analysis displayed TERF2 and RTA as two promising markers in disease diagnosis. In addition to that, Univariate analysis of clinico-pathological parameters and studied genes, TERF2 and RTA demonstrated significant association of these molecules in disease progression and are good predictor of disease course thus suggesting their utility in prognosis of MM.
Both GEM and CAP caused telomere shortening and increased expression of TRF2 with improved ascites in nude mice and decreased in vitro clonogenic activity. TRF2 knockdown altered telomeres to a shortened but new status that may evade XPF-dependent telomere loss and conferred resistance of SKOV3.ip1 ascites cells to low-dose GEM and CAP.
We demonstrate that promoter binding by TRF2 mediates PCGF3 promoter activity, and both the N-terminal and C-terminal domains of TRF2 are necessary for promoter activity
The reports the crystal structure of the N-terminal domain of TIN2 in complex with TIN2-binding motifs from TPP1 and TRF2, revealing how TIN2 interacts cooperatively with TPP1 and TRF2.
Both TRF1 and TRF2 were overexpressed in prostate cancer. There was no specificity of TRF2 in prostate cancer, while TRF1 may be associated with prostate cancer progression.
the excessive HULC plus MALAT1 reduced the methylation of the TERC promoter dependent on TRF2, increasing the TERC expression that causes the increase of interplay between TRET and TERC.
TERF2 knockdown by RNA interference had no effect on cell proliferation, migration, senescence and apoptosis. Instead, TERF2 knockdown increased the expression of cytokines implicated in inflammation and angiogenesis, except for vascular endothelial growth factor.
the telomere stability is under direct control of one of the major pro-oncogenic signaling pathways (RAS/RAF/MEK/ERK) via TRF2 phosphorylation.
the B-domain improves TRF2's interaction with DNA via enhanced long-range electrostatic interactions.
our findings describe TRF2 as a novel SIRT6 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 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 is down-regulated in the TRF2(DeltaBDeltaM)-induced senescence, which was mediated by ATM and p38 MAPK
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 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.
It plays a role in hematopoietic stem cell regulation and in the maintenance of the HSC pool and the development of hematological disorders.
shelterin subunits exhibit distinct spatiotemporal expression patterns, suggesting important tissue-specific functions during development and aging
Selective inactivation of Terf2 in neural progenitors induced apoptosis, resulting in a complete loss of the brain structure.
The authors propose that TRF2 masks and stabilizes the t-loop three-way junction, thereby protecting telomeres from detrimental deletions and PARP1 activation.
Overexpressing TRF2-S and silencing FMRP 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 platelet-derived growth factor receptor beta (PDGFRbeta).
role of TRF2 in skin homeostasis, is reported.
shelterin protein TIN2 can protect chromosome ends as a TRF2-tethered TIN2/TPP1/POT1 complex that lacks a physical connection to TRF1
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, Rap1, or the POT1 proteins (POT1a and POT1b) had no effect on the frequency of t-loop occurrence.
TAF7L associates with TRF2 both in vitro and in testis, suggesting that TAF7L 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 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
Mouse gene deletion experiments revealed DNA-damage-response pathways that threaten chromosome ends and how the components of the telomeric shelterin complex prevent activation of these pathways.[Shelterin]
TRF2 provides a crucial link between telomere function and ultraviolet-induced damage repair, whose alteration underlies genomic instability, cancer and aging.
PARP1 associates with telomere repeat binding factor 2 (TRF2) and is capable of poly(ADP-ribosyl)ation of TRF2, which affects binding of TRF2 to telomeric DNA.
with overexpressing the TRF2 telomere-binding protein, mice show short telomeres in the presence of telomerase activity, leading to premature aging and increased cancer
TRF2 and POT1 act independently to repress two DNA damage response pathways; TRF2 represses ATM, whereas POT1 prevents activation of ATR
The inactivation of TRF2ts at 37 degrees C was rapid and reversible, permitting induction of short periods (3-6 h) of telomere dysfunction in the G0, G1, and S/G2 phases of the cell cycle.
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