While all membranes share a characteristic bilayer morphology, their lateral organization can be remarkably complex. In biological membranes, lipids and proteins can self-assemble laterally to generate a variety of compositionally distinct domains that range in size from nanometers to microns, exist over a wide range of time scales, and assume varying curvatures and morphologies. Our group seeks to understand the physicochemical principles that govern the assembly and function of two related yet distinct classes of membrane nanodomains: membrane rafts and caveolae. Both caveolae and rafts reside within the plasma membrane of cells, form in a cholesterol-dependent manner, regulate multiple cellular processes, and, when defective, contribute to human disease. Current evidence suggests that rafts are small, dynamic, and primarily lipid-based. In contrast, caveolae are long-lived, morphologically well-defined, and built from specific protein components. Yet major questions still remain about how rafts and caveolae form and function. For example, only rudimentary approaches are currently available to manipulate rafts in cellular membranes. This represents a major roadblock to developing new approaches to study and control biological processes mediated by rafts or to modulate rafts for therapeutic purposes. For the case of caveolae, we now have in hand a parts list of the proteins required for their assembly. However, it is currently unknown how the protein caveolin- an essential structural component of caveolae- inserts into and bends membranes. In this talk, I will discuss our recent efforts to address these long-standing questions using a combination of chemical, biochemical, and structural approaches.

New approaches to uncover how membrane rafts and caveolae form and function

ACS Spring 2022

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