Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes?

@article{Nathan2013WhyDC,
  title={Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes?},
  author={James A Nathan and Hyoung Tae Kim and Lily Ting and Steven P Gygi and Alfred L Goldberg},
  journal={The EMBO journal},
  year={2013},
  volume={32 4},
  pages={552-65}
}
Although cellular proteins conjugated to K48-linked Ub chains are targeted to proteasomes, proteins conjugated to K63-ubiquitin chains are directed to lysosomes. However, pure 26S proteasomes bind and degrade K48- and K63-ubiquitinated substrates similarly. Therefore, we investigated why K63-ubiquitinated proteins are not degraded by proteasomes. We show that mammalian cells contain soluble factors that selectively bind to K63 chains and inhibit or prevent their association with proteasomes… CONTINUE READING
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The proteasomal

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