<br/>Protein protein interactions are an integral part of cell function and cell signaling. For example, cell surface proteins are important in cell activation through cis protein interactions as well as trans interactions for communication between two cells. Due to their important role in cell function, cell surface proteins are also widely researched as therapeutic targets. Therefore, it is important to understand this complex network of cis and trans interactions and the associated accessory and effector proteins. Proteomic analysis is a powerful way of mapping protein interactions. Common methods include, IP purification of protein complexes, covalent protein crosslinking of such complexes, and enzyme-based proximity labeling. The success of these approaches has led to the consideration of other chemical-based methods that are smaller in size, temporally controlled, and/or can avoid harsh treatment conditions. A remarkable example is the use of photocatalytic-based transformations whereby protein residues are labeled in the presence of visible light and a photocatalyst to probe cellular function. To this end, we have successfully developed a visible light activated labeling strategy for temporally-controlled membrane protein proximity labeling. This talk will describe the successful demonstration of this novel labeling technology on different cell types including cell line and patient derived three dimensional cell models with the end goal of identifying proteins with effector function.

Photoactivation based proximity labeling of cell surface receptor protein interactions

ACS Fall 2020 Virtual Meeting

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