Chapter title |
Proximity Ligation Assay: A Tool to Study Endogenous Interactions Between Tau and Its Neuronal Partners.
|
---|---|
Chapter number | 18 |
Book title |
Tau Protein
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-6598-4_18 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6596-0, 978-1-4939-6598-4
|
Authors |
Alexis Bretteville, Florie Demiautte, Julien Chapuis, Bretteville, Alexis, Demiautte, Florie, Chapuis, Julien |
Editors |
Caroline Smet-Nocca |
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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Demographic breakdown
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Researcher | 4 | 11% |
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Student > Master | 4 | 11% |
Other | 6 | 16% |
Unknown | 7 | 19% |
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Chemistry | 2 | 5% |
Other | 4 | 11% |
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