OptoPI3K, genetic code expansion, and click chemistry reveal mechanisms underlying reciprocal regulation between TRPV1 and PI3K.

ABSTRACT: Receptor tyrosine kinase signaling is characterized by complex webs of interconnected pathways that regulate diverse cellular functions. The complexity of signaling is a barrier to understanding the pathways that control any particular function. In this work, we use a novel combination of approaches and a new click chemistry probe to determine the role of one pathway in regulating cell surface expression of an ion channel and a receptor tyrosine kinase. We applied an optogenetic approach to uncouple activation of the PI3K pathway from other pathways downstream of RTK activation. In this context, we used genetic code expansion to introduce a click chemistry noncanonical amino acid into the extracellular side of membrane proteins. Applying a cell-impermeant click chemistry fluorophore allowe

SUBMITTER: Koh DS 

PROVIDER: S-EPMC10491195 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature