Mapping the dynamics and nanoscale organization of synaptic adhesion proteins using monomeric streptavidin

Ingrid Chamma, Mathieu Letellier, Corey Butler, Béatrice Tessier, Kok-Hong Lim, Isabel Gauthereau, Daniel Choquet, Jean-Baptiste Sibarita, Sheldon Park, Matthieu Sainlos () and Olivier Thoumine ()
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Ingrid Chamma: Interdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique
Mathieu Letellier: Interdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique
Corey Butler: Interdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique
Béatrice Tessier: Interdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique
Kok-Hong Lim: University at Buffalo
Isabel Gauthereau: Interdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique
Daniel Choquet: Interdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique
Jean-Baptiste Sibarita: Interdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique
Sheldon Park: University at Buffalo
Matthieu Sainlos: Interdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique
Olivier Thoumine: Interdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique

Nature Communications, 2016, vol. 7, issue 1, 1-15

Abstract: Abstract The advent of super-resolution imaging (SRI) has created a need for optimized labelling strategies. We present a new method relying on fluorophore-conjugated monomeric streptavidin (mSA) to label membrane proteins carrying a short, enzymatically biotinylated tag, compatible with SRI techniques including uPAINT, STED and dSTORM. We demonstrate efficient and specific labelling of target proteins in confined intercellular and organotypic tissues, with reduced steric hindrance and no crosslinking compared with multivalent probes. We use mSA to decipher the dynamics and nanoscale organization of the synaptic adhesion molecules neurexin-1β, neuroligin-1 (Nlg1) and leucine-rich-repeat transmembrane protein 2 (LRRTM2) in a dual-colour configuration with GFP nanobody, and show that these proteins are diffusionally trapped at synapses where they form apposed trans-synaptic adhesive structures. Furthermore, Nlg1 is dynamic, disperse and sensitive to synaptic stimulation, whereas LRRTM2 is organized in compact and stable nanodomains. Thus, mSA is a versatile tool to image membrane proteins at high resolution in complex live environments, providing novel information about the nano-organization of biological structures.

Date: 2016
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DOI: 10.1038/ncomms10773

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