[HTML][HTML] Inhibition of p97-dependent protein degradation by Eeyarestatin I
Q Wang, L Li, Y Ye - Journal of Biological Chemistry, 2008 - ASBMB
Elimination of misfolded proteins from the endoplasmic reticulum (ER) by ER-associated
degradation involves substrate retrotranslocation from the ER lumen into the cytosol for
degradation by the proteasome. For many substrates, retrotranslocation requires the action
of ubiquitinating enzymes, which polyubiquitinate substrates emerging from the ER lumen,
and of the p97-Ufd1-Npl4 ATPase complex, which hydrolyzes ATP to dislocate
polyubiquitinated substrates into the cytosol. Polypeptides extracted by p97 are eventually …
degradation involves substrate retrotranslocation from the ER lumen into the cytosol for
degradation by the proteasome. For many substrates, retrotranslocation requires the action
of ubiquitinating enzymes, which polyubiquitinate substrates emerging from the ER lumen,
and of the p97-Ufd1-Npl4 ATPase complex, which hydrolyzes ATP to dislocate
polyubiquitinated substrates into the cytosol. Polypeptides extracted by p97 are eventually …
