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Are Tau fibrils induced by phosphorylation and the interaction with 14-3-3 proteins relevant for Alzheimer disease?


Project Description

Several neurodegenerative diseases are associated with the formation of fibrous protein aggregates. The fibrillization of amyloid beta peptide into amyloid plaques and the agregation of hyperphosphorylated tau protein into neurofibrillar tangles are main neuropatological signs of Alzheimer disease. Studying of how different factors influence the formation of protein fibrils is the key for understanding this neurodegerative processes. The main aim of this PhD project will be preparation and analysis of tau fibrils prepared by variety of approaches. Major focus will be given on phosphorylation and interaction with 14-3-3 proteins. Interdisciplinary approach combining molecular biology and structural biology (mainly cryoEM tomography and AFM) methods will be applied. The described activities are part of international research projects allowing to spend the part of PhD study at the collaborative groups in Europe or North and South America and to learn specific research techniques, there.

Keywords: neurodegenerative diseases, Alzheimer disease, protein fibrils, phosphorylation state, 14-3-3 proteins, cryoEM tomography

HOW TO APPLY: Register for this call using the registration form at http://ls-phd.ceitec.cz/http-ls-phd-ceitec-cz/ and submit required documents to receive support with the preparation of the application and all formalities. Your application package will be forwarded to the supervisor for preliminary revision.
Applicants who wish to pursue a degree at the CEITEC PhD program must hold the equivalent of a Master’s degree (MSc) in similar field (four- or five-year undergraduate degree). The application can be submitted before obtaining the Master’s degree, however, the applicant should obtain the degree within five months after the application deadline.

Funding Notes

Admission for studies, student registration for the full-time study program and proper fulfillment of student duties constitute the student’s right to a regular income of 22 000 CZK (850 EUR). Information is available at View Website

Living costs and other practicalities available at View Website

References

1. Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., and Scheres, S. H. W. Cryo-EM structures of tau filaments from Alzheimer’s disease. Nature 2017, 547, 185–190
2. Falcon, B., Zhang, W., Murzin, A. G., Murshudov, G., Garringer, H. J., Vidal, R., Crowther, R. A., Ghetti, B., Scheres, S. H. W., and Goedert, M. Structures of filaments from Pick’s disease reveal a novel tau protein fold. Nature 2018, 561, 137–140
3. Zhang, W., Falcon, B., Murzin, A. G., Fan, J., Crowther, R. A., Goedert, M., and Scheres, S. H. Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases. eLife 2019, 8, e43584
4. Jansen, S.; Melková, K.; Trošanová, Z.; Hanáková, K.; Zachrdla, M.; Nováček, J.; Župa,E.; Zdráhal, Z.; Hritz, J.; Žídek, L.: Quantitative Mapping of MAP2c Phosphorylation and 14-3-3ζ Binding Sites Reveals Key Differences Between MAP2c and Tau. J. Biol. Chem. 2017, 292, 6715-6727
5. Melková, K.; Zapletal, V.; Narasimhan, S.; Jansen, S.; Hritz, J.; Škrabana, R.; Zweckstetter, M.; Ringkjøbing Jensen, M.; Blackledge, M.; Žídek, L. Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences. Biomolecules 2019, 9, 105.

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