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Role of phosphorylated 14-3-3 proteins

Project Description

14-3-3 proteins play key role in the neurobiochemistry of brain and are also associated with neurodegenerative amyloid diseases such as Alzheimer and Parkinson disease. 14-3-3 proteins bind more than 850 diverse target phosphoproteins, thereby forcing conformational changes or/and stabilizing active conformations in their target proteins. The main aim of this PhD project is to quantify extent of the phosphorylation of different isoforms of 14-3-3 protein family in different cell types. Subsequently, the potency of homo and heterodimerization involving the phosphorylated 14-3-3 proteins will be quantified by fluorescence, ITC and NMR biophysical assays. Finally, the impact on the binding of phosphorylated client proteins will be analyzed.

Keywords: Biophysical Chemistry, neurodegenerative diseases, phosphorylation state, 14-3-3 proteins, NMR, ITC, fluorescence

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


1. Sluchanko, N.N. Association of Multiple Phosphorylated Proteins with the 14-3-3 Regulatory Hubs: Problems and Perspectives. J. Mol. Biol. 2018, 430, 20–26.
2. Jandova, Z.; Trosanova, Z.; Weisova, V.; Oostenbrink, C.; Hritz, J. Free energy calculations on the stability of the 14-3-3 protein. BBA - Proteins and Proteomics, 2018, 1866, 442-450
3. Nagy, G., Oostenbrink, C., and Hritz, J. Exploring the binding pathways of the 14-3-3ζ protein: Structural and free-energy profiles revealed by Hamiltonian replica exchange molecular dynamics with distancefield distance restraints. PLoS One 2017, 12, 1–30.
4. Petr Louša, Hana Nedozrálová, Erik Župa, Jiří Nováček, Jozef Hritz: Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR. Biophysical Chemistry 2017, 223, 25-29
5. Hritz J.; Byeon I-J.; Krzysiak T.; Martinez A.; Sklenář V.; Gronenborn A.M. Dissection of binding between a phosphorylated tyrosine hydroxylase peptide and 14-3-3ζ: a complex story elucidated by NMR. Biophys. J. 2014, 107, 2185-2194

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