Abstract
Recent advances in the identification and analysis of protein–protein interaction complexes associated with synapses and synaptic proteins deepened not only our insights into the molecular composition and dynamic structural makeup of interneuronal connections but contributed also significantly to our understanding of the molecular and mechanistic aspects underlying functional plasticity in neuronal networks. In particular proteome analytical tools, combining traditional isolation protocols with modern mass spectrometric approaches, were utilized successfully for the molecular analysis of chemical synapses and other neuronal subcellular structures revealing new and exciting insights into the temporal and spatial changes of the proteins composing or associated with for example synaptic vesicles, synaptic membranes, or postsynaptic densities (PSDs). Proteomic approaches may thus offer also a chance to gain valuable insights into the so far elusive molecular composition of electrical synapses, the Cinderella fated and long neglected little brethren of “classical” chemical synapses. In this chapter we provide an experimental basis of how such an analysis can be designed, with a major focus on the most abundant electrical synapse protein, connexin36.
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Acknowledgment
We would like to thank Drs. Mamoru Matsubara, Stephanie Urschel, and Dirk Wolters for their kind and constructive support during mass spectrometric analysis and identification of protein-interaction partners and phosphorylation sites of Cx36.
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Alev, C., Zoidl, G., Dermietzel, R. (2013). Proteomic Approaches for the Study of Electrical Synapses and Associated Protein-Interaction Complexes. In: Dermietzel, R. (eds) The Cytoskeleton. Neuromethods, vol 79. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-266-7_7
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DOI: https://doi.org/10.1007/978-1-62703-266-7_7
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