Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Weitere Synonyme anzeigen
Wählen Sie die gewünschte Spezies
Human POT1 Protein expressed in HEK-293 Cells - ABIN2729370
Choi, Lakamp-Hawley, Kolar, Yan, Borgstahl, Ouellette: The OB-fold domain 1 of human POT1 recognizes both telomeric and non-telomeric DNA motifs. in Biochimie 2015
Show all 2 Pubmed References
Human HT1080 cells expressing POT1 D224N and lymphoblastoid cells carrying Y36H both showed increased telomere length and fragility in comparison to wild type cells. This strongly suggests that mutant POT1 causes chromosome instability and may play a role in lymphomagenesis in these families.
we propose that POT1 is a key factor regulating the balance between the efficiency and fidelity of nonhomologous end joining at non-telomeric DNA regions
POT1 was identified at 70 kDa in biopsy tissue of cervical cancer patients and its level was higher than that in normal cervical smears; the high level of POT1 in the biopsy tissue of cervical cancer patients showed the influence of this shelterin component in cervical carcinogenesis and also cell immortalization
A defective POT1-TPP1 complex leads to longer and fragile telomeres, which in turn promotes genomic instability and cancer.
several missense mutations in human cancers that disrupt the POT1C-TPP1 interaction, resulting in POT1 instability, were identified.
melanoma associated POT1 germline variants seem to be rare.
Results indicate that lenti-shRNA-mediated POT1-KD significantly reduced POT1 mRNA and protein expression. POT1-KD immediately downregulated c-Myc expression, which led to the inhibition of cell proliferation, tumorigenesis, and HDACi response
A role of POT1 germline mutations in cancer predisposition beyond melanoma development
study suggests that, gallstone does not affect telomere length and even after having increased telomere length, decreased expression of some shelterin genes in inflamed tissue might cause telomeres to cap improperly, possibly leading to telomere dysfunction and further, gallbladder carcinogenesis
loss-of-function mutations in protection of telomeres 1 (POT1) co-segregated with Chronic lymphocytic leukemia.
hPOT1 OB-folds are required to protect and prevent newly replicated telomeres from engaging in Alternative non-homologous end joining mediated fusions that would otherwise promote genome instability to fuel tumorigenesis.
the study identifies mutations in KRAS and POT1 as novel determinants of outcome after chemoimmunotherapy using chlorambucil and anti-CD20 treatment.
Lung fibroblasts deficient in Sirt1 or treated with a selective Sirt1 inhibitor exhibit increased cellular senescence and decreased TPP1 levels, whereas Sirt1 overexpression and pharmacological activation protect against CS-induced TPP1 reduction and telomeric DNA damage.
Binding of POT1-TPP1 unfolds telomere secondary structure to assist loading of additional heterodimers.
We found that NEK6-mediated phosphorylation of TPP1 Ser255 in G2/M phase regulates the association between telomerase activity and TPP1. Furthermore, we found evidence that POT1 negatively regulates TPP1 phosphorylation because the level of Ser255 phosphorylation was elevated when telomeres were elongated by a POT1 mutant lacking its OB-fold domains
Coats plus is caused by a defect in POT1/CST-dependent telomere fill-in
Downregulation of Protection of Telomeres 1 expression in myelodysplastic syndromes with 7q deletion.
The conservation between fission yeast Tpz1-Pot1 and human TPP1-POT1 interactions resulted in mapping a human melanoma-associated POT1 mutation (A532P) to the TPP1-POT1 interface.
Missense variant p.R117C is associated with cardiac angiosarcoma in TP-53 negative Li-Fraumeni-like families. Mutation carriers show reduced telomere-bound POT1 levels, abnormally long telomeres and increased telomere fragility.
OB-fold domain 1 of human POT1 recognizes both telomeric and non-telomeric DNA motifs
The tissue expression analysis indicated that the swine POT1 gene is differentially expressed in tissues including muscle, heart, liver, fat, kidney, lung, pancreas and spleen.
nearly identical POT1b subunit of shelterin has been shown to be much less proficient than POT1a in repression of ATR
The telomere binding protein POT1a inhibits the production of reactive oxygen species, and rejuvenates aged hematopoietic stem cells.
proliferation of cancer cells lacking POT1 is enabled by the attenuation of the ATR kinase pathway.
demonstrated that cells expressing TIN2DeltaTPP1 instead of wild-type TIN2 phenocopy the POT1a,b knockout setting without showing additional phenotypes
The results of this study found telomere uncapping by Pot1a inactivation resulted in an Atm-dependent loss of cerebellar interneurons and granule neuron precursors in the mouse nervous system. The
shelterin protein TIN2 can protect chromosome ends as a TRF2-tethered TIN2/TPP1/POT1 complex that lacks a physical connection to TRF1
Simultaneous inactivation of Pot1a and p53 resulted in endometrial intraepithelial carcinoma-like lesions in transgenic mice.
Telomere protection by TPP1/POT1 requires tethering to TIN2.
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]
POT1a degradation resulted in rapid and reversible activation of the ATR pathway in G1 and S/G2.
The ability of mPot1 to unfold the antiparallel tetraplex of the mouse telomeric DNA is required for telomerase-mediated telomere elongation.
TPP1 deletion resulted in the release of POT1a and POT1b from chromatin and loss of these proteins from telomeres, indicating that TPP1 is required for the telomere association of POT1a and POT1b but not for their stability.
Our results suggest that POT1a is crucial for the maintenance of both telomere integrity and overall genomic stability.
We conclude that mouse telomeres require two distinct POT1 proteins whereas human telomeres have one.
shRNA mediated depletion of endogenous Pot1b in Pot1a deficient cells resulted in increased chromosomal aberrations
Tpp1 is required for the protective function of Pot1 proteins.
TRF2 and POT1 act independently to repress two DNA damage response pathways; TRF2 represses ATM, whereas POT1 prevents activation of ATR
Tripeptidyl peptidase I (Tpp1) confers telomere end protection by recruiting Pot1a and Pot1b to telomeres.
The ability of Pot1 to unfold the antiparallel tetraplex of the telomeric DNA may be important for regulation of telomerase-mediated telomere elongation.
This gene is a member of the telombin family and encodes a nuclear protein involved in telomere maintenance. Specifically, this protein functions as a member of a multi-protein complex that binds to the TTAGGG repeats of telomeres, regulating telomere length and protecting chromosome ends from illegitimate recombination, catastrophic chromosome instability, and abnormal chromosome segregation. Increased transcriptional expression of this gene is associated with stomach carcinogenesis and its progression. Alternatively spliced transcript variants have been described.
POT1-like telomere end-binding protein
, protection of telomeres 1 homolog
, protection of telomeres protein 1
, POT1 protection of telomeres 1 homolog
, single-strand telomeric DNA-binding protein
, POT1 protection of telomeres 1 homolog (S. pombe)
, protection of telomeres 1
, protection of telomeres 1 homolog (S. pombe)
, protection of telomeres protein 1-like
, protection of telomeres 1A