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

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.

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Guillén Boixet , Jordina 1, Autor
Kopach , Andrii 1, Autor
Holehouse, Alex S.1, Autor
Wittmann , Sina 1, Autor
Jahnel, Marcus 1, Autor
Schlüssler, Raimund1, Autor
Kim, Kyoohyun2, Autor
Trussina , Irmela 1, Autor
Wang , Jie1, Autor
Mateju , Daniel 1, Autor
Poser, Ina1, Autor
Maharana , Shovamayee 1, Autor
Ruer , Martine 1, Autor
Richter , Doris 1, Autor
Zhang , Xiaojie1, Autor
Chang , Young-Tae1, Autor
Guck, Jochen2, 3, Autor           
Honigmann , Alf 1, Autor
Mahamid , Julia 1, Autor
Hyman , Anthony A. 1, Autor
Pappu, Rohid V.1, AutorAlberti , Simon 1, AutorFranzmann , Titus 1, Autor mehr..
Affiliations:
1external , ou_persistent22              
2Guck Division, Max Planck Institute for the Science of Light, Max Planck Society, ou_3164416              
3Max-Planck-Zentrum für Physik und Medizin, Max Planck Institute for the Science of Light, Max Planck Society, ou_3164414              

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 Zusammenfassung: 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.

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Sprache(n): eng - English
 Datum: 2020-03-202020-04-16
 Publikationsstatus: Online veröffentlicht
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: DOI: 10.1016/j.cell.2020.03.049
 Art des Abschluß: -

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Titel: Cell
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: Cambridge, USA : CELL PRESS
Seiten: 15 Band / Heft: 181 (2) Artikelnummer: - Start- / Endseite: 346 - 361 Identifikator: ISSN: 0092-8674