Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling.

@article{Varadan2004SolutionCO,
  title={Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling.},
  author={Ranjani Varadan and Michael Assfalg and Aydin Haririnia and Shahri Raasi and Cecile M. Pickart and David Fushman},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 8},
  pages={7055-63}
}
Diverse cellular events are regulated by post-translational modification of substrate proteins via covalent attachment of one or a chain of ubiquitin molecules. The outcome of (poly)ubiquitination depends upon the specific lysine residues involved in the formation of polyubiquitin chains. Lys48-linked chains act as a universal signal for proteasomal degradation, whereas Lys63-linked chains act as a specific signal in several non-degradative processes. Although it has been anticipated that… CONTINUE READING

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