Abstract
Tau is a microtubule associated protein (MAP) that is expressed in neurons of the central nervous system. Tau proteins are deregulated in a group of pathologies, including Alzheimer’s disease, commonly called tauopathies. Therefore intensive research has been conducted to understand both the regulation of Tau and its involvement in neuronal cellular pathways. Since its originally described interactor tubulin, Tau has been described to interact with several other proteins, including tyrosine kinases (Src, Fyn, Lck) and Phospholipase C-γ. In this chapter, we describe the use of proximity ligation assay as a versatile method to study the endogenous interaction of Tau with these different neuronal partners and use the recently identified Tau interactor Bin1 as case study.
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Acknowledgments
We thank the BioImaging Center Lille-Nord de France (BICeL) facility (Lille, France). We also thank the Albert Einstein College of Medicine of Yeshiva University (New York, USA) for the kind gift of Tau-phosphorylation -dependent antibodies. This work is funded by the French government’s LABEX DISTALZ (development of innovative strategies for a transdisciplinary approach to Alzheimer’s disease) and the US Alzheimer’s association (IIRG-06-25487).
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Bretteville, A., Demiautte, F., Chapuis, J. (2017). Proximity Ligation Assay: A Tool to Study Endogenous Interactions Between Tau and Its Neuronal Partners. In: Smet-Nocca, C. (eds) Tau Protein. Methods in Molecular Biology, vol 1523. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6598-4_18
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DOI: https://doi.org/10.1007/978-1-4939-6598-4_18
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