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TZAP competed with the shelterin complex component telomere repeat binding factor TRF2 for telomere binding, and elevated TRF2 expression reduced TZAP binding to telomeres, providing a mechanism by which TZAP might preferentially associate with long telomeres.
our findings describe TRF2 as a novel SIRT6 (show SIRT6 Proteins) 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 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
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 (show PARP1 Proteins) activation.
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.
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