Matrisome Biology Seminar - M. Florencia Sánchez

Ligand-free in situ confinement for GPCR activation and signal transduction

Cell-cell communication and signal transduction rely on the assembly of receptorlig and complexes at the plasma membrane. The spatiotemporal receptor organization plays a pivotal role in evoking cellular responses. Nevertheless, the mechanism for cluster formation and how their localization within the plasma membrane influence cell responses is not comprehensively understood. Thus, traceless modifications with high spatiotemporal control that allow fine tuning of protein networks in a fast, reversible, and non-invasive manner are required. Here, by establishing modular matrices with a multivalent high-affinity nanotool, we rewired in situ the lateral membrane organization of the hormone neuropeptide Y2 receptor in living cells by light. Within seconds, receptor clustering can be modulated in size, location, and density. By in situ confinement, changes in cellular morphology, motility, and calcium signaling revealed a ligand-independent receptor activation. Overall, the matrix as well as the employed nanotool represent versatile instruments for tracking of cellular processes and depict now the possibility to elucidate unexplored mechanisms in cell signaling and mechanotransduction.

This seminar is organized by the interdiciplinary FRIAS Research Group MatrixCode: matrisome pathology

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