The polymerizing protein actin is a principal component of the cytoskeleton and plays a central role in the transport and localization of molecules within a cell. While monomeric actin is relatively inert, the polymer binds many other intracellular proteins, thereby scaffolding molecular interaction networks into highly localized reaction centers that are specific to locally required functions. Despite the importance of actin, the tools available to study it in cells are surprisingly limited. I will present here two advances in the fluorescence microscopy of actin. The first utilizes fluorescence polarization anisotropy to image the polymerization state and dynamics of actin in live cells. The second, Serial Target Interaction Microscopy (STIM), reconstructs the spatial distribution of interactions between a single protein and a large number of other proteins. Using STIM we have generated the first spatial maps of a partial actin protein interactome. While I will focus here on its application to actin, STIM represents a promising general approach to bridge the gap between microscopy and molecular systems biology.


Wednesday, March 25, 2015, 12:00. Seminar Room

Hosted by Prof. Turgut Durduran