Single-molecule tracking of tau reveals fast kiss-and-hop interaction with microtubules in living neurons

DC FieldValueLanguage
dc.contributor.authorJanning, Dennis
dc.contributor.authorIgaev, Maxim
dc.contributor.authorSuendermann, Frederik
dc.contributor.authorBruehmann, Joerg
dc.contributor.authorBeutel, Oliver
dc.contributor.authorHeinisch, Juergen J.
dc.contributor.authorBakota, Lidia
dc.contributor.authorPiehler, Jacob
dc.contributor.authorJunge, Wolfgang
dc.contributor.authorBrandt, Roland
dc.date.accessioned2021-12-23T16:01:52Z-
dc.date.available2021-12-23T16:01:52Z-
dc.date.issued2014
dc.identifier.issn10591524
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/5213-
dc.description.abstractThe microtubule-associated phosphoprotein tau regulates microtubule dynamics and is involved in neurodegenerative diseases collectively called tauopathies. It is generally believed that the vast majority of tau molecules decorate axonal microtubules, thereby stabilizing them. However, it is an open question how tau can regulate microtubule dynamics without impeding microtubule-dependent transport and how tau is also available for interactions other than those with microtubules. Here we address this apparent paradox by fast single-molecule tracking of tau in living neurons and Monte Carlo simulations of tau dynamics. We find that tau dwells on a single microtubule for an unexpectedly short time of similar to 40 ms before it hops to the next. This dwell time is 100-fold shorter than previously reported by ensemble measurements. Furthermore, we observed by quantitative imaging using fluorescence decay after photoactivation recordings of photoactivatable GFP-tagged tubulin that, despite this rapid dynamics, tau is capable of regulating the tubulin-microtubule balance. This indicates that tau's dwell time on microtubules is sufficiently long to influence the lifetime of a tubulin subunit in a GTP cap. Our data imply a novel kiss-and-hop mechanism by which tau promotes neuronal microtubule assembly. The rapid kiss-and-hop interaction explains why tau, although binding to microtubules, does not interfere with axonal transport.
dc.description.sponsorshipstate of Lower SaxonyEuropean Commission; Bundesministerium fur Bildung und Forschung (KMU-innovativ-7)Federal Ministry of Education & Research (BMBF); Z-project [SFB944]; We thank Vanessa Herkenhoff for technical help, Rainer Kurre for assistance with microscopy devices, and Christian P. Richter for providing the code for localization and tracking. W.J. holds a Niedersachsen-Professur, awarded by the state of Lower Saxony. This work was supported by the Bundesministerium fur Bildung und Forschung (KMU-innovativ-7; R.B.) and the Z-project of the SFB944.
dc.language.isoen
dc.publisherAMER SOC CELL BIOLOGY
dc.relation.ispartofMOLECULAR BIOLOGY OF THE CELL
dc.subjectALZHEIMERS-DISEASE
dc.subjectBINDING
dc.subjectCell Biology
dc.subjectCELLS
dc.subjectGROWTH
dc.subjectLOCALIZATION
dc.subjectMEMBRANE
dc.subjectMESSENGER-RNA
dc.subjectORGANIZATION
dc.subjectPROTEIN-TAU
dc.subjectTRANSPORT
dc.titleSingle-molecule tracking of tau reveals fast kiss-and-hop interaction with microtubules in living neurons
dc.typejournal article
dc.identifier.doi10.1091/mbc.E14-06-1099
dc.identifier.isiISI:000344236800019
dc.description.volume25
dc.description.issue22, SI
dc.description.startpage3541
dc.description.endpage3551
dc.contributor.orcid0000-0001-8781-1604
dc.contributor.orcid0000-0002-8777-5006
dc.contributor.orcid0000-0003-0101-1257
dc.contributor.researcheridG-3801-2017
dc.contributor.researcheridH-6108-2018
dc.identifier.eissn19394586
dc.publisher.place8120 WOODMONT AVE, STE 750, BETHESDA, MD 20814-2755 USA
dcterms.isPartOf.abbreviationMol. Biol. Cell
dcterms.oaStatusGreen Published, hybrid
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.orcid0000-0003-0101-1257-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidPiJa938-
crisitem.author.netidJuWo587-
crisitem.author.netidBrRo587-
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