TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres.

@article{Chang2003TRF1ID,
  title={TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres.},
  author={William Gee Chang and Jasmin N. Dynek and Susan Smith},
  journal={Genes & development},
  year={2003},
  volume={17 11},
  pages={1328-33}
}
Mammalian telomeres are coated by the sequence-specific, DNA-binding protein, TRF1, a negative regulator of telomere length. Previous results showed that ADP-ribosylation of TRF1 by tankyrase 1 released TRF1 from telomeres and promoted telomere elongation. We now show that loss of TRF1 from telomeres results in ubiquitination and degradation of TRF1 by the proteasome and that degradation is required to keep TRF1 off telomeres. Ubiquitination of TRF1 is regulated by its telomere-binding status… CONTINUE READING