AI Article Synopsis
- The study focuses on caveolin, a monotopic membrane protein that forms complexes essential for creating caveolae, which are small, flask-shaped invaginations in the plasma membrane that detect membrane tension.
- Using cryo-electron microscopy, researchers discovered that caveolin-1 is made up of 11 protomers arranged in a disc-like structure, providing insights into its unique mechanism of interacting with membranes and how specific regions of caveolin-1 contribute to its role.
Article Abstract
Membrane-sculpting proteins shape the morphology of cell membranes and facilitate remodeling in response to physiological and environmental cues. Complexes of the monotopic membrane protein caveolin function as essential curvature-generating components of caveolae, flask-shaped invaginations that sense and respond to plasma membrane tension. However, the structural basis for caveolin's membrane remodeling activity is currently unknown. Here, we show that, using cryo-electron microscopy, the human caveolin-1 complex is composed of 11 protomers organized into a tightly packed disc with a flat membrane-embedded surface. The structural insights suggest a previously unrecognized mechanism for how membrane-sculpting proteins interact with membranes and reveal how key regions of caveolin-1, including its scaffolding, oligomerization, and intramembrane domains, contribute to its function.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9094659 | PMC |
| http://dx.doi.org/10.1126/sciadv.abn7232 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!