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복잡계자기조립연구단
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RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by CondensationHighly Cited Paper

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dc.contributor.authorGuillen-Boixet J.-
dc.contributor.authorKopach A.-
dc.contributor.authorHolehouse A.S.-
dc.contributor.authorWittmann S.-
dc.contributor.authorJahnel M.-
dc.contributor.authorSchlussler R.-
dc.contributor.authorKim K.-
dc.contributor.authorTrussina I.R.E.A.-
dc.contributor.authorWang J.-
dc.contributor.authorMateju D.-
dc.contributor.authorPoser I.-
dc.contributor.authorMaharana S.-
dc.contributor.authorRuer-Gruss M.-
dc.contributor.authorRichter D.-
dc.contributor.authorZhang X.-
dc.contributor.authorYoung-Tae Chang-
dc.contributor.authorGuck J.-
dc.contributor.authorHonigmann A.-
dc.contributor.authorMahamid J.-
dc.contributor.authorHyman A.A.-
dc.contributor.authorPappu R.V.-
dc.contributor.authorAlberti S.-
dc.contributor.authorFranzmann T.M.-
dc.date.available2020-07-06T06:42:25Z-
dc.date.created2020-04-20-
dc.date.issued2020-04-
dc.identifier.issn0092-8674-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/7131-
dc.description.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-
dc.language영어-
dc.publisherCell Press-
dc.titleRNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000526184900016-
dc.identifier.scopusid2-s2.0-85083031389-
dc.identifier.rimsid71904-
dc.contributor.affiliatedAuthorYoung-Tae Chang-
dc.identifier.doi10.1016/j.cell.2020.03.049-
dc.identifier.bibliographicCitationCell, v.181, no.2, pp.346 - 361.e17-
dc.relation.isPartOfCell-
dc.citation.titleCell-
dc.citation.volume181-
dc.citation.number2-
dc.citation.startPage346-
dc.citation.endPage361.e17-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryCell Biology-
dc.subject.keywordPlusMESSENGER-RNA-
dc.subject.keywordPlusPHASE-SEPARATION-
dc.subject.keywordPlusDISORDERED PROTEIN-
dc.subject.keywordPlusTRANSLATION-
dc.subject.keywordPlusTOMOGRAPHY-
dc.subject.keywordPlusPRINCIPLES-
dc.subject.keywordPlusCONTRIBUTE-
dc.subject.keywordPlusDYNAMICS-
dc.subject.keywordPlusREVEALS-
dc.subject.keywordPlusFORM-
dc.subject.keywordAuthorstress granules-
dc.subject.keywordAuthorstress response-
dc.subject.keywordAuthorG3BP-
dc.subject.keywordAuthorliquid-to-solid transition-
dc.subject.keywordAuthorNeurodegenerative disease-
dc.subject.keywordAuthorphase separation-
dc.subject.keywordAuthorRNP granules-
Appears in Collections:
Center for Self-assembly and Complexity(복잡계 자기조립 연구단) > 1. Journal Papers (저널논문)
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1-s2.0-S0092867420303421-main.pdfDownload

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