Caveolae are highly abundant membrane micro-domains forming invaginations at the plasma membrane of many mammalian cells. They are involved in various cellular processes including endocytosis, cell motility, lipid homeostasis, signalling, pathogen entry and cancer. Structural information about the caveolar architecture has remained enigmatic. The three major structural coat proteins include the integral membrane protein caveolin, and the peripherally attached cavin and EHD2 proteins. They form large, independently assembled complexes on the cytosolic face of caveolae.
The objective of our study is to identify structural domains of the cavin complex and residues within the protein that confer specificity of binding to lipids and cavin assembly into a large native complex. We purified cavin coat complexes from mammalian cells and analyzed their structure in solution and after reconstitution into liposomes. In parallel, caveolae were imaged in situ in vitrified cells by cryo electron tomography. Our results lead to a new model of caveolar coat assembly and reveal insights on how caveolae induce membrane curvature.
Pascale Schellenberger did her PhD at The University of Strasbourg under the supervision of Dr. Christophe Ritzenthaler (IBMP, Strasbourg) and Dr. Oliver Lemaire (INRA, Colmar) working on Plant virology with an emphasis on structural biology. In 2010, she joined Pr. Kay Grünewald’s group at the University of Oxford to develop correlative light and electron tomography on frozen hydrated samples at high resolution. She is currently interested in membrane remodelling with a focus on the Caveolar coat structures and Adenovirus entry mechanism.
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