Abstract

Receptor tyrosine kinases (RTKs) are an important class of transmembrane proteins that serve an integral role in cell signaling. These RTKs are implicated in tumor development which makes them an appealing target for drug discovery. These receptors are activated upon oligomerization in the plasma membrane. As the receptors laterally self-associate and form dimers/higher order oligomers, they can auto-phosphorylate distinct tyrosine residues and become activated. In addition, prior studies suggest that the location and distribution of the receptors in the plasma membranes can regulate activity. Traditional microscopy methods to study oligomerization are limited due to diffraction limited resolution. Instead, we utilize single-molecule localization microscopy (SMLM) to visualize distributions of fluorescently labeled receptors. Spatial analysis of EphA2 super resolution images shows ligand-induced changes in distributions of the receptors in the membrane.

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