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Cited 30 time in webofscience Cited 43 time in scopus
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RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation

Title
RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation
Authors
Guillen-Boixet, JordinaKopach, AndriiHolehouse, Alex S.Wittmann, SinaJahnel, MarcusSchluessler, RaimundKim, KyoohyunTrussina, Irmela R. E. A.Wang, JieMateju, DanielPoser, InaMaharana, ShovamayeeRuer-Gruss, MartineRichter, DorisZhang, XiaojieChang, Young-TaeGuck, JochenHonigmann, AlfMahamid, JuliaHyman, Anthony A.Pappu, Rohit V.Alberti, SimonFranzmann, Titus M.
Date Issued
Apr-2020
Publisher
CELL PRESS
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, G3BPadopts 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 hetero-typic multivalent interactions may be a general principle underlying RNP granule assembly.
URI
http://oasis.postech.ac.kr/handle/2014.oak/103886
ISSN
0092-8674
Article Type
Article
Citation
CELL, vol. 181, no. 2, page. 346 - +, 2020-04
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