Nanoscopic anatomy of dynamic multi-protein complexes at membranes resolved by graphene-induced energy transfer

DC FieldValueLanguage
dc.contributor.authorFuellbrunn, Nadia
dc.contributor.authorLi, Zehao
dc.contributor.authorJorde, Lara
dc.contributor.authorRichter, Christian P.
dc.contributor.authorKurre, Rainer
dc.contributor.authorLangemeyer, Lars
dc.contributor.authorYu, Changyuan
dc.contributor.authorMeyer, Carola
dc.contributor.authorEnderlein, Jorg
dc.contributor.authorUngermann, Christian
dc.contributor.authorPiehler, Jacob
dc.contributor.authorYou, Changjiang
dc.date.accessioned2021-12-23T16:16:35Z-
dc.date.available2021-12-23T16:16:35Z-
dc.date.issued2021
dc.identifier.issn2050084X
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/11943-
dc.description.abstractInsights into the conformational organization and dynamics of proteins complexes at membranes is essential for our mechanistic understanding of numerous key biological processes. Here, we introduce graphene-induced energy transfer (GIET) to probe axial orientation of arrested macromolecules at lipid monolayers. Based on a calibrated distance-dependent efficiency within a dynamic range of 25 nm, we analyzed the conformational organization of proteins and complexes involved in tethering and fusion at the lysosome-like yeast vacuole. We observed that the membrane-anchored Rab7-like GTPase Ypt7 shows conformational reorganization upon interactions with effector proteins. Ensemble and time-resolved single-molecule GIET experiments revealed that the HOPS tethering complex, when recruited via Ypt7 to membranes, is dynamically alternating between a `closed' and an `open' conformation, with the latter possibly interacting with incoming vesicles. Our work highlights GIET as a unique spectroscopic ruler to reveal the axial orientation and dynamics of macromolecular complexes at biological membranes with subnanometer resolution.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [INST 190/146-3 (SFB944-P8), EXC 2067/1-390729940, INST 190/182-1, INST 190/149-3 (SFB944P11), INST190/152-3 (SFB944-Z), UN 111/12-1, YO 166/1-1]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31870976]; Osnabrueck University; Deutsche Forschungsgemeinschaft INST 190/146-3 (SFB944-P8) Jacob Piehler; National Natural Science Foundation of China 31870976 Zehao Li Changyuan Yu; Intramural funding from Osnabrueck University Integrated Science Carola Meyer Christian Ungermann Jacob Piehler Changjiang You; Deutsche Forschungsgemeinschaft EXC 2067/1-390729940 Jorg Enderlein; Deutsche Forschungsgemeinschaft INST 190/182-1 Rainer Kurre Jacob Piehler; Deutsche Forschungsgemeinschaft INST 190/149-3 (SFB944P11) Christian Ungermann; Deutsche Forschungsgemeinschaft INST190/152-3 (SFB944-Z) Jacob Piehler; Deutsche Forschungsgemeinschaft UN 111/12-1 Christian Ungermann; Deutsche Forschungsgemeinschaft YO 166/1-1 Changjiang You; The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
dc.language.isoen
dc.publisherELIFE SCIENCES PUBLICATIONS LTD
dc.relation.ispartofELIFE
dc.subjectBINDING
dc.subjectBiology
dc.subjectDNA
dc.subjectFUSION
dc.subjectHOPS
dc.subjectIDENTIFICATION
dc.subjectLife Sciences & Biomedicine - Other Topics
dc.subjectLOCALIZATION
dc.subjectMICROSCOPY
dc.subjectORIENTATION
dc.subjectRAB GTPASE
dc.subjectRECEPTOR INTERACTIONS
dc.titleNanoscopic anatomy of dynamic multi-protein complexes at membranes resolved by graphene-induced energy transfer
dc.typejournal article
dc.identifier.doi10.7554/eLife.62501
dc.identifier.isiISI:000614370500001
dc.description.volume10
dc.contributor.orcid0000-0001-5091-7157
dc.contributor.orcid0000-0002-4309-0910
dc.contributor.orcid0000-0003-0851-2767
dc.contributor.orcid0000-0002-7839-6397
dc.contributor.researcheridI-1723-2012
dc.publisher.placeSHERATON HOUSE, CASTLE PARK, CAMBRIDGE, CB3 0AX, ENGLAND
dcterms.isPartOf.abbreviationeLife
dcterms.oaStatusGreen Published, gold
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptSonderforschungsbereich 944: Physiologie und Dynamik zellulärer Mikrokompartimente-
crisitem.author.deptidfb05-
crisitem.author.deptidfb04-
crisitem.author.deptidfb05-
crisitem.author.deptidorganisation19-
crisitem.author.orcid0000-0002-6872-6567-
crisitem.author.orcid0000-0003-0851-2767-
crisitem.author.orcid0000-0002-2143-2270-
crisitem.author.orcid0000-0002-7839-6397-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgFB 05 - Biologie/Chemie-
crisitem.author.grandparentorgUniversität Osnabrück-
crisitem.author.netidKuRa617-
crisitem.author.netidMeCa197-
crisitem.author.netidEnJo001-
crisitem.author.netidUnCh999-
crisitem.author.netidPiJa938-
crisitem.author.netidYoCh745-
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