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Membrane remodeling by the caveolin-1 8s oligomeric complex
Hrushikesh Malshikare1, Durba Sengupta1
1Physical and Materials Chemistry Division, CSIR-National Chemical Laboratory, Pune, Maharashtra, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, India.
Biophysical Journal
|August 24, 2025
Summary
Caveolin-1 oligomers interact with cell membranes, altering lipid organization and membrane curvature. This interaction depends on membrane structure, influencing caveolin-1
Area of Science:
- Cell Biology
- Biophysics
- Structural Biology
Background:
- Caveolin-1 is a key scaffolding protein forming caveolae, essential for cellular processes.
- Recent cryo-EM studies revealed the 8S oligomeric structure of caveolin-1.
- Understanding caveolin-1's membrane interactions is crucial for elucidating its function.
Purpose of the Study:
- To investigate the membrane interactions of oligomeric caveolin-1.
- To explore how caveolin-1 affects lipid organization in different membrane environments.
- To determine the role of membrane topology and curvature in caveolin-1 function.
Main Methods:
- Coarse-grained molecular dynamics simulations.
- Modeling of palmitoylated and nonpalmitoylated caveolin-1.
- Simulations on multicomponent lipid bilayers and vesicles.
Main Results:
- Caveolin-1 oligomers bind to membranes in a shallow, monotopic arrangement.
- Lipid remodeling occurs around the bound caveolin-1 complex.
- Membrane curvature induction differs between vesicles and planar bilayers, affecting lipid clustering.
Conclusions:
- Caveolin-1's functional dynamics are significantly influenced by lipid organization and membrane topology.
- Caveolin-1 plays a dual role in sensing and inducing membrane curvature.
- These findings provide insights into caveolin-1's involvement in cellular processes mediated by membrane dynamics.
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