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Updated: Apr 28, 2026
Author Spotlight: Exploring Plasma Membrane Repair Mechanisms with Innovative Thermoplasmonic Puncturing
Published on: January 19, 2024
Sorcin couples Annexin A11 recruitment and ESCRT-III assembly during plasma membrane repair
Jordan Matthew Ngo1, Justin Krish Williams1,2, Abinayaa Murugupandiyan1
1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720.
Abstract:
The absence of a cell wall affords animal cells diverse functionality at the cost of acute sensitization to plasma membrane (PM) damage. Thus, animal cells tightly monitor and maintain the integrity of their PM to prevent cell death. Genetic loss of PM repair factors is associated with human diseases including muscular dystrophy and neurodegeneration. Despite evidence that annexin and endosomal sorting complex required for transport (ESCRT) proteins are required for PM repair, the extent to which their recruitment is coordinated at sites of membrane damage is unclear. Here, we identify sorcin as a new PM repair factor that directly couples annexin A11 (ANXA11)-mediated sensing of PM damage and ESCRT-III assembly. We demonstrate that ANXA11, recruited to the PM upon damage-induced calcium influx, serves as an anchor that facilitates the sequential recruitment of sorcin and ESCRT-III at PM lesions. Our data highlight mechanistic and topological similarities between the budding of membrane-enveloped viruses and damage-induced microvesicles. We propose that they share a common mechanism of membrane budding and speculate that membrane-enveloped viruses may have co-opted this host pathway of PM ESCRT recruitment to facilitate virion assembly and propagation.
Insights
Animal cells lack cell walls, making plasma membrane (PM) repair crucial. Sorcin acts as a novel factor, coordinating annexin A11 and ESCRT-III recruitment for efficient PM repair.
Area of Science:
- Cell Biology
- Membrane Biology
- Biochemistry
Background:
- Animal cells, lacking a protective cell wall, are vulnerable to plasma membrane (PM) damage.
- Maintaining PM integrity is vital for cell survival, and its disruption is linked to diseases like muscular dystrophy and neurodegeneration.
- Annexin and ESCRT proteins are known PM repair factors, but their coordinated recruitment remains unclear.
Purpose of the Study:
- To identify novel factors involved in PM repair.
- To elucidate the coordination mechanism between annexin and ESCRT proteins during PM repair.
- To explore potential links between PM repair pathways and viral propagation.
Main Methods:
- Investigated the role of sorcin in PM repair.
- Utilized calcium influx assays to study PM damage response.
- Examined the recruitment dynamics of annexin A11 (ANXA11), sorcin, and ESCRT-III at sites of PM damage.
Main Results:
- Identified sorcin as a novel PM repair factor.
- Demonstrated that ANXA11 acts as an anchor, sequentially recruiting sorcin and ESCRT-III to damaged PM sites.
- Showcased similarities between virus budding and damage-induced microvesicle formation.
Conclusions:
- Sorcin directly links ANXA11-mediated PM damage sensing to ESCRT-III assembly.
- The study proposes a shared membrane budding mechanism between viral propagation and cellular repair processes.
- Viruses may exploit host PM ESCRT recruitment pathways for their assembly and spread.
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