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hal.structure.identifierCentre d'Etudes Nucléaires de Bordeaux Gradignan [CENBG]
hal.structure.identifierUniversité de Bordeaux [UB]
dc.contributor.authorDOMART, Florelle
hal.structure.identifierEuropean Synchrotron Radiation Facility [ESRF]
dc.contributor.authorCLOETENS, Peter
hal.structure.identifierCentre d'Etudes Nucléaires de Bordeaux Gradignan [CENBG]
dc.contributor.authorROUDEAU, Stephane
hal.structure.identifierCentre d'Etudes Nucléaires de Bordeaux Gradignan [CENBG]
dc.contributor.authorCARMONA, Asuncion
hal.structure.identifierUniversité de Bordeaux [UB]
dc.contributor.authorVERDIER, Emeline
hal.structure.identifierUniversité de Bordeaux [UB]
dc.contributor.authorCHOQUET, Daniel
hal.structure.identifierCentre d'Etudes Nucléaires de Bordeaux Gradignan [CENBG]
dc.contributor.authorORTEGA, Richard
dc.date.accessioned2022-04-19T12:21:49Z
dc.date.available2022-04-19T12:21:49Z
dc.date.issued2020
dc.identifier.issn2050-084X
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/136858
dc.description.abstractEn<jats:p>Zinc and copper are involved in neuronal differentiation and synaptic plasticity but the molecular mechanisms behind these processes are still elusive due in part to the difficulty of imaging trace metals together with proteins at the synaptic level. We correlate stimulated-emission-depletion microscopy of proteins and synchrotron X-ray fluorescence imaging of trace metals, both performed with 40 nm spatial resolution, on primary rat hippocampal neurons. We reveal the co-localization at the nanoscale of zinc and tubulin in dendrites with a molecular ratio of about one zinc atom per tubulin-αβ dimer. We observe the co-segregation of copper and F-actin within the nano-architecture of dendritic protrusions. In addition, zinc chelation causes a decrease in the expression of cytoskeleton proteins in dendrites and spines. Overall, these results indicate new functions for zinc and copper in the modulation of the cytoskeleton morphology in dendrites, a mechanism associated to neuronal plasticity and memory formation.</jats:p>
dc.language.isoen
dc.publishereLife Sciences Publication
dc.title.enCorrelating STED and synchrotron XRF nano-imaging unveils cosegregation of metals and cytoskeleton proteins in dendrites
dc.typeArticle de revue
dc.identifier.doi10.7554/elife.62334
dc.subject.halPhysique [physics]
bordeaux.journaleLife
bordeaux.pagee62334
bordeaux.volume9
bordeaux.hal.laboratoriesCentre d'Études Nucléaires de Bordeaux Gradignan (CENBG)*
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionCNRS
bordeaux.peerReviewedoui
hal.identifierhal-03136706
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-03136706v1
bordeaux.COinSctx_ver=Z39.88-2004&amp;rft_val_fmt=info:ofi/fmt:kev:mtx:journal&amp;rft.jtitle=eLife&amp;rft.date=2020&amp;rft.volume=9&amp;rft.spage=e62334&amp;rft.epage=e62334&amp;rft.eissn=2050-084X&amp;rft.issn=2050-084X&amp;rft.au=DOMART,%20Florelle&amp;CLOETENS,%20Peter&amp;ROUDEAU,%20Stephane&amp;CARMONA,%20Asuncion&amp;VERDIER,%20Emeline&amp;rft.genre=article


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