PhD project: Physiological role of cation/proton antiporters in monovalent cation homeostasis
The tight regulation of intracellular ion concentrations is crucial for all cells. Optimal levels of cations are ensured by the coordinated activity of various transporters. If the activity of ion transporters and consequently ion homeostasis are disordered, it results in many pathological processes. Among the cation transport systems that participate in ensuring the optimal intracellular level of alkali-metal cations and protons (pH) in cells of most organisms are cation/H+ exchangers (CPA/SLC9 family). The PhD study will be dedicated to the characterization of cation/proton exchangers from yeasts and mammals with the aim of (i) determining new structural and functional elements in these proteins, (ii) identifying new types of their activity regulation, and (iii) identifying so far unknown proteins that participate in their biogenesis and degradation. The results will provide new insights into the cell cation-homeostasis regulatory network in the unicellular model eukaryotic organism and will serve to identify corresponding regulatory mechanisms in higher eukaryotes.
Candidate’s profile (requirements):
The candidate should be fluent in English, highly self-motivated with master's degree or equivalent (obtained before October 2019) in molecular biology, biochemistry, microbiology or related fields. Experience in basic laboratory (PCR, DNA electrophoresis, bacteria transformation, plasmid isolation) and bioinformatics (DNA and protein sequence search and comparison, sequenced fragments analysis, plasmid and primers design) techniques is an advantage.
Kinclova-Zimmermannová O., Falson P., Cmunt D., Sychrova H. A hydrophobic filter confers the cation selectivity of Zygosaccharomyces rouxii plasma-membrane Na+/H+ antiporters. J. Mol. Biol. 427: 1681-1694 (2015).
Rosas-Santiago P., Lagunas-Gomez D., Yáñez-Domínguez C., Vera-Estrella R., Zimmermannová O., Sychrová H., Pantoja O.: Plant and yeast cornichon possess a conserved acidic motif required for correct targeting of plasma membrane cargos. BBA Mol. Cell. Res. 1864(10):1809-1818 (2017).
Rosas-Santiago P., Zimmermannova O., Vera-Estrella R., Sychrová H., Pantoja O.: Erv14 cargo receptor participates in yeast salt tolerance via its interaction with the plasma-membrane Nha1 cation/proton antiporter. BBA 1858(1):67-74 (2016).
Kinclova-Zimmermannova O., Zavrel M., Sychrova H.: Importance of the seryl and threonyl residues of the fifth transmembrane domain to the substrate specificity of yeast plasma membrane Na+/H+ antiporters. Mol. Membr. Biol. 23(4):349-61 (2006).
Kinclova-Zimmermannova O., Zavrel M., Sychrova H.: Identification of conserved prolyl residue important for transport activity and the substrate specificity range of yeast plasma membrane Na+/H+ antiporters. J. Biol. Chem. 280(34):30638-47 (2005).
Supervisor: Olga Zimmermannová, Ph.D.