Analysis of Tau/Nucleoporin Interactions by Surface Plasmon Resonance Spectroscopy
| العنوان: | Analysis of Tau/Nucleoporin Interactions by Surface Plasmon Resonance Spectroscopy |
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| المؤلفون: | Lisa Diez, Larisa E. Kapinos, Roderick Y. H. Lim, Susanne Wegmann |
| المصدر: | New York, NY : Springer US, Methods in Molecular Biology 2551, 95-109 (2023). doi:10.1007/978-1-0716-2597-2_8 Protein Aggregation / Cieplak, Andrzej Stanisław (Editor) ; New York, NY : Springer US, 2023, Chapter 8 ; ISSN: 1064-3745=1940-6029 ; ISBN: 978-1-0716-2596-5=978-1-0716-2597-2 ; doi:10.1007/978-1-0716-2597-2 Methods in Molecular Biology ISBN: 9781071625965 |
| بيانات النشر: | Springer US, 2023. |
| سنة النشر: | 2023 |
| مصطلحات موضوعية: | metabolism [Nuclear Pore Complex Proteins], Spectrum Analysis, metabolism [Nuclear Pore], Proteins, physiology [Active Transport, Cell Nucleus], tau Proteins, metabolism [tau Proteins], Biacore, Nup98, Nuclear Pore Complex Proteins, Surface plasmon resonance (SPR), ddc:570, chemistry [Proteins], MAPT, methods [Surface Plasmon Resonance], Tau, Nuclear pore complex (NPC) |
| الوصف: | Tau, a soluble and predominantly neuronal protein, is best known for its microtubule (MT)-binding function in the cytosol, where it decisively contributes to stability as well as modulation of MT dynamics. In Alzheimer's disease and other tauopathies, Tau is altered into forming intracellular neurofibrillary tangles; additionally, also a mislocalization from the cytosol to the nucleus has been observed where interactions of Tau with the nucleus become possible. Using surface plasmon resonance (SPR), it was recently shown that Tau can directly interact with certain nucleoporins (e.g., Nup98), components of the nuclear pore complex (NPC). The NPC constitutes large regulated pores in the nuclear envelope that facilitate the bidirectional exchange of proteins, nucleic acids, and other biomolecules between the inner section of the nucleus and the cytosol, the nucleocytoplasmic transport. The mechanism of Tau/Nup interactions is as yet unknown, and a systematic interaction analysis of Tau with different Nups can be of high value to decipher the molecular binding mechanism of Tau to Nups. SPR is a useful tool to analyze binding affinities and kinetic parameters in a label-free environment. While one interaction partner is immobilized on a sensor chip, the second is supplied within a constant flow of buffer. Binding of mobile molecules to immobilized ones changes the refractive index of the medium close to the sensor surface with the signal being proportional to the bound mass. In this chapter, we describe the application of the SPR technique for the investigation of Tau binding to nucleoporins. |
| اللغة: | English |
| ردمك: | 978-1-07-162596-5 |
| DOI: | 10.1007/978-1-0716-2597-2_8 |
| DOI: | 10.1007/978-1-0716-2597-2 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e777ba461e2c7b59cc939f24412a100d https://pub.dzne.de/record/165566 |
| Rights: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....e777ba461e2c7b59cc939f24412a100d |
| قاعدة البيانات: | OpenAIRE |
| ردمك: | 9781071625965 |
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| DOI: | 10.1007/978-1-0716-2597-2_8 |