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Journal Article

RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation

MPS-Authors

Kim,  Kyoohyun
Guck Division, Max Planck Institute for the Science of Light, Max Planck Society;

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Guck,  Jochen
Guck Division, Max Planck Institute for the Science of Light, Max Planck Society;
Guck Division, Max-Planck-Zentrum für Physik und Medizin, Max Planck Institute for the Science of Light, Max Planck Society;

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Citation

Guillén Boixet, J., Kopach, A., Holehouse, A. S., Wittmann, S., Jahnel, M., Schlüssler, R., et al. (2020). RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation. Cell, 181(2), 346-361. doi:10.1016/j.cell.2020.03.049.


Cite as: https://hdl.handle.net/21.11116/0000-0006-5587-2
Abstract
Stressed cells shut down translation, release mRNA molecules from polysomes, and form stress granules (SGs) via a network of interactions that involve G3BP. Here we focus on the mechanistic underpinnings of SG assembly. We show that, under non-stress conditions, G3BP adopts a compact auto-inhibited state stabilized by electrostatic intramolecular interactions between the intrinsically disordered acidic tracts and the positively charged arginine-rich region. Upon release from polysomes, unfolded mRNAs outcompete G3BP auto-inhibitory interactions, engendering a conformational transition that facilitates clustering of G3BP through protein-RNA interactions. Subsequent physical crosslinking of G3BP clusters drives RNA molecules into networked RNA/protein condensates. We show that G3BP condensates impede RNA entanglement and recruit additional client proteins that promote SG maturation or induce a liquid-to-solid transition that may underlie disease. We propose that condensation coupled to conformational rearrangements and heterotypic multivalent interactions may be a general principle underlying RNP granule assembly.