Ubiquitin Ligase RLIM Modulates Telomere Length Homeostasis through a Proteolysis of TRF1.

@article{Her2009UbiquitinLR,
  title={Ubiquitin Ligase RLIM Modulates Telomere Length Homeostasis through a Proteolysis of TRF1.},
  author={Yoon Ra Her and I. K. Chung},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 13},
  pages={8557-66}
}
The telomeric protein TRF1 negatively regulates telomere length by inhibiting telomerase access at the telomere termini, suggesting that the protein level of TRF1 at telomeres is tightly regulated. Regulation of TRF1 protein abundance is essential for proper telomere function and occurs primarily through post-translational modifications of TRF1. Here we describe RLIM, a RING H2 zinc finger protein with intrinsic ubiquitin ligase activity, as a TRF1-interacting protein. RLIM increases TRF1… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 24 extracted citations

References

Publications referenced by this paper.

Ubiquitin-mediated Proteolysis of TRF1 by RLIM

  • A. Follenzi, L. E. Ailles, S. Bakovic, M. Geuna, L. andNaldini
  • MARCH 27,
  • 2000

Similar Papers

Loading similar papers…