Analysis of Npl4 deletion mutants in mammalian cells unravels new Ufd1-interacting motifs and suggests a regulatory role of Npl4 in ERAD.

@article{Lass2008AnalysisON,
  title={Analysis of Npl4 deletion mutants in mammalian cells unravels new Ufd1-interacting motifs and suggests a regulatory role of Npl4 in ERAD.},
  author={Agnieszka Lass and Elizabeth J. McConnell and Krista Fleck and Alla Palamarchuk and Cezary W{\'o}jcik},
  journal={Experimental cell research},
  year={2008},
  volume={314 14},
  pages={2715-23}
}
Npl4 is a 67 kDa protein forming a stable heterodimer with Ufd1, which in turn binds the ubiquitous p97/VCP ATPase. According to a widely accepted model, VCP(Ufd1-Npl4) promotes the retrotranslocation of emerging ER proteins, their ubiquitination by associated ligases, and handling to the 26S proteasome for degradation in a process known as ERAD (ER-associated degradation). Using a series of Npl4 deletion mutants we have revealed that the binding of Ufd1 to Npl4 is mediated by two regions: a… CONTINUE READING

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