Ubiquitin- and ATP-dependent unfoldase activity of P97/VCP•NPLOC4•UFD1L is enhanced by a mutation that causes multisystem proteinopathy.

@article{Blythe2017UbiquitinAA,
  title={Ubiquitin- and ATP-dependent unfoldase activity of P97/VCP•NPLOC4•UFD1L is enhanced by a mutation that causes multisystem proteinopathy.},
  author={Emily E Blythe and Kristine C. Olson and Vincent Chau and Raymond J Deshaies},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2017},
  volume={114 22},
  pages={
          E4380-E4388
        }
}
p97 is a "segregase" that plays a key role in numerous ubiquitin (Ub)-dependent pathways such as ER-associated degradation. It has been hypothesized that p97 extracts proteins from membranes or macromolecular complexes to enable their proteasomal degradation; however, the complex nature of p97 substrates has made it difficult to directly observe the fundamental basis for this activity. To address this issue, we developed a soluble p97 substrate-Ub-GFP modified with K48-linked ubiquitin chains… CONTINUE READING
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