Molecular Architecture of the Human Caveolin-1 Complex

Overview

Journal Sci Adv

Specialties Biology
Science

Date 2022 May 11

PMID 35544577

Authors

Jason C Porta

Bing Han

Alican Gulsevin

Jeong Min Chung

Yelena Peskova

Sarah Connolly

Hassane S Mchaourab

Jens Meiler

Erkan Karakas

Anne K Kenworthy

Melanie D Ohi

Affiliations

Soon will be listed here.

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.

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