The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome.

@article{Jacobson2009TheL4,
  title={The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome.},
  author={Andrew D. Jacobson and Nan-yan Zhang and Ping Xu and Ke-Jun Han and Seth M. Noone and Junmin Peng and Chang-Wei Liu},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 51},
  pages={35485-94}
}
The role of Lys-63 ubiquitin chains in targeting proteins for proteasomal degradation is still obscure. We systematically compared proteasomal processing of Lys-63 ubiquitin chains with that of the canonical proteolytic signal, Lys-48 ubiquitin chains. Quantitative mass spectrometric analysis of ubiquitin chains in HeLa cells determines that the levels of Lys-63 ubiquitin chains are insensitive to short-time proteasome inhibition. Also, the Lys-48/Lys-63 ratio in the 26 S proteasome-bound… CONTINUE READING

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EMBO Rep . 10 , 466 – 473 Differential Proteasomal Processing of Lys - 48 and - 63 Ubiquitin Chains

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