CDC13 Antibody

1. DNA binding by Cdc13 employs a highly cooperative interface whereby sequence diversity is accommodated through plastic binding modes. PMID: 30249661
2. The core Cdc13 ssDNA-binding activity is wholly contained within a single tight-binding oligosaccharide/oligonucleotide/oligopeptide binding (OB)-fold. PMID: 24057216
3. Dimerization of the OB2 domain of Cdc13 is required for proper Cdc13, Stn1, Ten1 (CST) assembly and productive telomere capping. PMID: 23177925
4. Cdc13, and a S314D mutation negatively affected telomere length. Our findings provide new targets in Cdc13 - a key telomerase regulatory protein for modulation of telomere dynamics PMID: 23181431
5. regulated binding of Cdc13 to chromosome termini dictates subsequent interaction of a recruitment-competent telomerase complex with telomeres PMID: 23390975
6. show that both Cdc48 and Vms1, but not Cdc48 cofactors Ufd1 and Ufd2, are crucial for the degradation of Cdc13, a telomere regulator PMID: 22718752
7. Cdc13 SUMOylation restrains telomerase functions by promoting Cdc13 interaction with the telomerase inhibitor Stn1 without affecting end protection. PMID: 21743457
8. Cdc13-Pol1 interaction revealed multiple mechanisms by which dimerization regulates telomere lengths in vivo. PMID: 20877309
9. results are inconsistent with a model in which the Cdc13-Est1 interaction is regulated by Tel1-mediated phosphorylation of the Cdc13 telomerase recruitment domain; an alternative model is proposed for the role of Tel1 in telomere homeostasis PMID: 20837994
10. Deletion of SGS1 and the nuclease EXO1 reduces resection at uncapped telomeres and together with deletion of RAD9 permits cell survival without CDC13. PMID: 20808892
11. Data present a structural, biochemical, and functional characterization of Cdc13. PMID: 20837709
12. Mec1, the ATR ortholog, couples the detection of DNA ends with the inhibition of telomerase. Mec1 inhibits telomere healing by phosphorylating Cdc13 on its S306 residue, a phosphorylation event that suppresses Cdc13 accumulation at double-strand breaks PMID: 20194442
13. the telomeric overhang is recognized with high affinity (3 pM) and sequence specificity by the essential protein Cdc13, which coordinates end-capping and telomerase activities at the telomere PMID: 16411763
14. Neither Cdc13 nor its partner Stn1 are necessary for telomere capping if nuclease activities that are active at uncapped telomeres are attenuated. PMID: 16767084
15. Results demonstrate that the telomerase recruitment domain of Cdc13p as an important new telomere-specific target of Mec1p/Tel1p. PMID: 17108359
16. Lys568 is also located on the DNA-binding surface of Cdc13p PMID: 17166094
17. Results suggest that the Cdc13 telomere cap coordinates Mec1 and Tel1 accumulation rather than simply covering the DNA ends at telomeres. PMID: 17377065
18. identified distinct Stn1p domains that mediate interaction with either Ten1p or Cdc13p, allowing analysis of whether the interaction between Cdc13p and Stn1p is indeed essential for telomere capping or length regulation PMID: 17947422
19. The binding of ssDNA to Cdc-13 induces localized conformational changes in a previously unappreciated region of the protein distant from the binding site. PMID: 18250086
20. A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied cellular processes influencing telomere capping in Saccharomyces cerevisiae PMID: 18845848
21. Rad24-2 truncation protein affects telomere structure or recombination in a manner distinct from rad24-delta. PMID: 18948753
22. Cdk1-dependent phosphorylation of Cdc13 is essential for efficient recruitment of the yeast telomerase complex to telomeres by favoring the interaction of Cdc13 with Est1 rather than the competing Stn1-Ten1 complex. PMID: 19135888

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KEGG: sce:YDL220C

STRING: 4932.YDL220C