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Updated: Nov 23, 2025

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
Published on: March 14, 2019
Cdc48/Shp1 participates in dissociation of protein complexes to regulate their activity
Linda Lauinger1, Karin Flick1, Peter Kaiser2
1Department of Biological Chemistry, School of Medicine, University of California Irvine, 240D Med Sci I, Irvine, CA 92697-1700, USA.
Abstract:
The AAA-ATPase p97/Cdc48 is one of the most abundant proteins in eukaryotes, and owing to its multiple functions, is considered the swiss army knife of cells. Recent findings demonstrate that p97/Cdc48 and its cofactor p47/Shp1 control the heavy metal stress response by active, signal-triggered disassembly of a multisubunit ubiquitin ligase. Here we review this pathway and describe recently achieved mechanistic insight into the role of p47/Shp1 in this process.
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