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

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Title
RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation
Author(s)
Guillen-Boixet J.; Kopach A.; Holehouse A.S.; Wittmann S.; Jahnel M.; Schlussler R.; Kim K.; Trussina I.R.E.A.; Wang J.; Mateju D.; Poser I.; Maharana S.; Ruer-Gruss M.; Richter D.; Zhang X.; Young-Tae Chang; Guck J.; Honigmann A.; Mahamid J.; Hyman A.A.; Pappu R.V.; Alberti S.; Franzmann T.M.
Publication Date
2020-04
Journal
Cell, v.181, no.2, pp.346 - 361.e17
Publisher
Cellpress
Abstract
© 2020 The Author(s)Reconstitution of stress granule assembly reveals an autoinhibitory conformation of G3BP that is alleviated by RNA binding, demonstrating how this central node of the stress granule network phase-separates in response to rising cellular RNA concentrations. © 2020 The Author(s)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
URI
https://pr.ibs.re.kr/handle/8788114/7131
ISSN
0092-8674
Appears in Collections:
Center for Self-assembly and Complexity(복잡계 자기조립 연구단) > Journal Papers (저널논문)
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