Impact of reactive oxygen species on surface localization of membrane proteins

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Cells interact with one other and with their surroundings through proteins that reside at the cell surface. Proteins located at the surface of the cell play a role in forming connections that hold cells together, responding to the chemicals and hormones our bodies produce, responding to drugs and in many other processes. These proteins do not remain fixed in one location, but in many cases, they move around both within the cell surface membrane allowing complex interactions with other proteins, as well as to and from the surface membrane allowing control over their availability. Some of this movement is controlled by the formation of caveolae. Caveolae are invaginations in the cell membrane that can act as “signaling domains” or can bud off to remove proteins from the surface. Caveolin-1 is a caveolae-associated scaffolding protein that can be activated by reactive oxygen species (ROS) such as hydrogen peroxide. One of the main sources of reactive oxygen species in cells is a family of enzymes called NADPH oxidases, or NOX enzymes. We aim to define the relationship between NADPH oxidase derived ROS, caveolin-1 phosphorylation and activation, movement of cell surface proteins.