Protein proximity labeling is a powerful technique for the unbiased assessment of protein-protein interactions or bystander proteins with effector function.  A number of enzyme-based strategies have been developed over the last 10 years that either generate a reactive labeling species in proximity to the protein of interest, or physically "stamp" neighboring proteins.  The success of these approaches has led to the consideration of other chemical-based methods that are smaller in size, can be temporally controlled, and/or can avoid harsh treatment conditions.  One notable example is the use of photocatalytic-based transformations whereby protein residues are labeled in the presence of visible light and a photocatalyst to alter protein activity and/or probe cellular function.  To this end, we have successfully developed a visible light-activated tyrosine 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 and protein targets with the end goal of identifying proteins with effector function. <br/>

Mapping of immunomodulatory receptor protein interactions via photocatalytic-based proximity labeling of the cell surface

2019 Spring National Meeting

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