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Updated: Jan 19, 2026
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Reconstitution of Msp1 Extraction Activity with Fully Purified Components
Published on: August 10, 2021
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New ATPase regulators--p97 goes to the PUB
Louise Madsen1, Michael Seeger, Colin A Semple
1Department of Biology, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen Ø, Denmark.
Summary
The p97/VCP (also known as Cdc48) ATPase complex interacts with cofactors to regulate cellular processes. PUB-domain proteins act as adaptors, with their p97 association controlled by tyrosine phosphorylation.
Area of Science:
- Cellular Biology
- Molecular Mechanisms
- Protein Interactions
Background:
- The AAA-type ATPase complex p97/VCP (mammals) or Cdc48 (yeast) is crucial for diverse cellular functions.
- p97's functions, including membrane fusion and protein degradation, are mediated by specific cofactors.
- Over 20 p97 cofactors are known, with expanding roles linked to the ubiquitin system.
Purpose of the Study:
- To provide an overview of PUB-domain proteins and other p97-interacting proteins.
- To highlight the role of PUB-domain proteins as p97 adaptors.
- To discuss the regulation of p97 cofactor interaction by tyrosine phosphorylation.
Main Methods:
- Literature review of PUB-domain proteins and p97 interactors.
- Analysis of protein domains and regulatory mechanisms.
- Synthesis of current understanding of p97 cofactor functions.
Main Results:
- PUB-domain proteins represent a conserved family of p97 adaptors.
- Tyrosine phosphorylation regulates the association of PUB-domain proteins with p97.
- This regulation suggests a role as a signaling relay between pathways and p97.
Conclusions:
- PUB-domain proteins are key regulators of p97/VCP (Cdc48) function.
- Tyrosine phosphorylation-mediated signaling integrates with p97-dependent cellular processes.
- Further research into these interactions will elucidate fundamental cellular mechanisms.
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