ArticleScience advances2025
ASPL couples the assembly of stress granules with their VCP-mediated disassembly.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Stress granules at the crossroads of the proteostasis network.RNA biology · 2026Review
- BOULE is Essential for the Dynamic Disassembly of Heat Shock Granules in Male Germ Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The p97 adaptor p47/NSFL1C is necessary for stress granule dissolution after heat stress.bioRxiv : the preprint server for biology · 2026Article
- ASPL-driven subunit exchange remodels VCP/p97 hexamers and is impaired by a multisystem proteinopathy mutation.bioRxiv : the preprint server for biology · 2026Article
- Proximity proteomics reveals OTUD6B regulation of stress granule dynamics through coalescence with VCP/p97.Cell death & disease · 2026Article
- Pharmacological modulation of stress granulesFrontiers in pharmacology · 2026Review
Corrections and comments
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Authors and funding
26 authors.
Funding
Abstract
Stress granules (SGs) are dynamic RNA-protein assemblies that form in response to cellular stress and must be efficiently disassembled to restore normal cell function. Valosin-containing protein (VCP), an enzyme implicated in neurodegenerative diseases, is essential for SG disassembly, but whether and how this process is coordinated with SG assembly remains unclear. Here, we identify the VCP cofactor, Alveolar soft part sarcoma locus (ASPL) as a key regulator linking SG assembly and disassembly. ASPL promotes SG assembly by facilitating biomolecular condensation of Ras guanosine triphosphatase-activating protein-binding protein (G3BP) and stabilizing its interactions with other SG proteins. ASPL also facilitates phosphorylation and activation of VCP by UNC-51-like kinases 1 and 2 (ULK1/2), enabling G3BP extraction and efficient SG disassembly. Pathogenic VCP mutations that disrupt ASPL binding impair SG disassembly, a defect rescued by phosphomimetic mutations or ASPL depletion. Our findings suggest that disruptions in the ASPL-VCP interaction uncouple SG assembly and disassembly, representing a potential mechanism underlying VCP-associated neurodegenerative diseases.
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