Single-molecule imaging reveals dynamic biphasic partition of RNA-binding proteins in stress granules

DC FieldValueLanguage
dc.contributor.authorNiewidok, Benedikt
dc.contributor.authorIgaev, Maxim
dc.contributor.authorda Graca, Abel Pereira
dc.contributor.authorStrassner, Andre
dc.contributor.authorLenzen, Christine
dc.contributor.authorRichter, Christian P.
dc.contributor.authorPiehler, Jacob
dc.contributor.authorKurre, Rainer
dc.contributor.authorBrandt, Roland
dc.date.accessioned2021-12-23T16:01:51Z-
dc.date.available2021-12-23T16:01:51Z-
dc.date.issued2018
dc.identifier.issn00219525
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/5205-
dc.description.abstractStress granules (SGs) are cytosolic, nonmembranous RNA-protein complexes. In vitro experiments suggested that they are formed by liquid-liquid phase separation; however, their properties in mammalian cells remain unclear. We analyzed the distribution and dynamics of two paradigmatic RNA-binding proteins (RBPs), Ras GTPase-activating protein SH3-domain-binding protein (G3BP1) and insulin-like growth factor II mRNA-binding protein 1 (IMP1), with single-molecule resolution in living neuronal cells. Both RBPs exhibited different exchange kinetics between SGs. Within SGs, single-molecule localization microscopy revealed distributed hotspots of immobilized G3BP1 and IMP1 that reflect the presence of relatively immobile nanometer-sized nanocores. We demonstrate alternating binding in nanocores and anomalous diffusion in the liquid phase with similar characteristics for both RBPs. Reduction of low-complexity regions in G3BP1 resulted in less detectable mobile molecules in the liquid phase without change in binding in nanocores. The data provide direct support for liquid droplet behavior of SGs in living cells and reveal transient binding of RBPs in nanocores. Our study uncovers a surprising disconnect between SG partitioning and internal diffusion and interactions of RBPs.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB 944]; This work was supported by Deutsche Forschungsgemeinschaft (grant SFB 944, project P1, to R. Brandt and J. Piehler).
dc.language.isoen
dc.publisherROCKEFELLER UNIV PRESS
dc.relation.ispartofJOURNAL OF CELL BIOLOGY
dc.subjectBODIES
dc.subjectCell Biology
dc.subjectCELLS
dc.subjectCOMPLEXES
dc.subjectDISEASE
dc.subjectIDENTIFICATION
dc.subjectLIQUID DROPLETS
dc.subjectLOCALIZATION MICROSCOPY
dc.subjectMESSENGER-RNA
dc.subjectPHASE-TRANSITIONS
dc.subjectTRACKING
dc.titleSingle-molecule imaging reveals dynamic biphasic partition of RNA-binding proteins in stress granules
dc.typejournal article
dc.identifier.doi10.1083/jcb.201709007
dc.identifier.isiISI:000428997800015
dc.description.volume217
dc.description.issue4
dc.description.startpage1303
dc.description.endpage1318
dc.contributor.orcid0000-0001-8781-1604
dc.contributor.orcid0000-0003-0101-1257
dc.contributor.researcheridH-6108-2018
dc.identifier.eissn15408140
dc.publisher.place950 THIRD AVE, 2ND FLR, NEW YORK, NY 10022 USA
dcterms.isPartOf.abbreviationJ. Cell Biol.
dcterms.oaStatushybrid, Green Published
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0002-2143-2270-
crisitem.author.orcid0000-0002-6872-6567-
crisitem.author.orcid0000-0003-0101-1257-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidPiJa938-
crisitem.author.netidKuRa617-
crisitem.author.netidBrRo587-
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