Clipping or Extracting: Two Ways to Membrane Protein Degradation.
Heidelberg, Germany. In Trends Cell Biol, Oct 2015
While most of our understanding of this mechanism comes from studies on p97/Cdc48-mediated protein dislocation along the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, recent studies have revealed intramembrane proteolysis to be an additional mechanism that can extract transmembrane segments.
Control of p97 function by cofactor binding.
Würzburg, Germany. In Febs Lett, Oct 2015
p97 (also known as Cdc48, Ter94, and VCP) is an essential, abundant and highly conserved ATPase driving the turnover of ubiquitylated proteins in eukaryotes.
ESCRT-III controls nuclear envelope reformation.
Bristol, United Kingdom. In Nature, Jul 2015
How annular fusion is accomplished is unknown, but it is thought to involve the p97 AAA-ATPase complex and bears a topological equivalence to the membrane fusion event that occurs during the abscission phase of cytokinesis.
Proteotoxic crisis, the ubiquitin-proteasome system, and cancer therapy.
Pasadena, United States. In Bmc Biol, 2013
Here, I consider possible explanations for this apparently limited applicability, and discuss whether inhibiting other broadly acting components of the ubiquitin-proteasome system - including ubiquitin-activating enzyme and the AAA-ATPase p97/VCP - might be more generally effective in cancer therapy.