Understanding Periperal Membrane Protein Interactions | BPS Thematic Meeting

Understanding Peripheral Membrane Protein Interactions: Structure, Dynamics, Function and Therapy

Monday Speaker Abstracts

PEEKING OUT FROM INSIDE THE MEMBRANE: THE CURIOUS CASE OF CAVEOLINS Anne K. Kenworthy ; 1 University of Virginia, Mol Physiol Biol Phys, Charlottesville, VA, USA Peripheral membrane proteins typically associate with one leaflet of the membrane. This characteristic is shared with monotopic membrane proteins that enter and exit the same side of the bilayer. Here, I will discuss the unusual structural features of caveolins, a family of monotopic membrane proteins located on the cytoplasmic face of the plasma membrane. Caveolins are best known for their role as building blocks of caveolae, flask-shaped invaginations that sense and relay signals and protect cells from stress. Classically, caveolins have been suggested to sit at the membrane-water interface, with large portions of the protein projecting into the cytoplasm. In contrast, our recent cryoEM structure reveals caveolins form an amphipathic disc that is predicted to be deeply embedded in the membrane. I will discuss how this unique structural organization helps shape membranes to promote caveolae assembly, impacts the ability of caveolins to serve as signaling and sensing hot spots, and serves as a conserved structural framework across the tree of life.

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