Our Laboratory is focused on structural biology (the relationship between the structure and function of certain groups of proteins), particularly we focus on the proteins which participate in the signal transmission in the cell. Among methods we use are recombinant protein expression, biophysical characterization, study of intermolecular interactions, protein structure and interaction surfaces. All these methods enable us to better understand the details how the activity and function of protein-protein complexes is regulated. Our research is focused mainly on:
- Structural biology of 14-3-3 proteins and their complexes
- Mechanism of regulation of proteinkisases CaMKK1, CaMKK2 and ASK1
- Study of inhibition of protease caspase-2 and ligase Nedd4-2 by 14-3-3 protein
- Study of DNA-binding domain of transcription factor FOXO4
EXTERNAL WEBSITE OF THE LABORATORY
Projects
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Phosducin (Pdc), a highly conserved phosphoprotein, plays an important role in the regulation of G-protein signalling, transcriptional control, and modulation of blood pressure. Pdc is negatively regulated by phosphorylation followed by binding to the 14-3-3 protein.
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Our results show the activation of yeast neutral trehalase Nth1 by 14-3-3 proteins from the structural point of view. Our data could be important for understanding of the activation process of Nth1 as well as of the role of 14-3-3 proteins in the regulation of other enzymes.
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Achievements
Two accepted papers in Communications Biology: July and August 2021
Pavel Pohl, Rohit Joshi, Olivia Petrvalska, Tomas Obsil and Veronika Obsilova
14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains | Communications Biology (nature.com)
Commun. Biol. 2021 July 22; 4(1):899.
Matej Horvath, Olivia Petrvalska, Petr Herman, Tomas Obsil and Veronika Obsilova
14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites | Communications Biology (nature.com)
Commun. Biol. 2021 August 19; 4(1):986.
IF = 6.268
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The study published in prestigious journal eLife identifies small molecule compounds that interact with the Forkhead box O3 transcription factor (FOXO3) and modulate its activity.
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Publications
Neves; J. F. - Petrvalská; Olivia - Bosica; F. - Cantrelle; F. X. - Merzougui; H. - O'Mahony; G. - Hanoulle; X. - Obšil; Tomáš - Landrieu; I.
Phosphorylated full-length Tau interacts with 14-3-3 proteins via two short phosphorylated sequences; each occupying a binding groove of 14-3-3 dimer
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FEBS Journal. 2021; 288(6); 1918-1934
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IF = 5.542
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Boušová; Kristýna - Bednárová; Lucie - Zouharová; Monika - Vetýšková; Veronika - Poštulková; Klára - Hofbauerová; Kateřina - Petrvalská; Olivia - Vaněk; O. - Tripsianes; K. - Vondrášek; Jiří
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The order of PDZ3 and TrpCage in fusion chimeras determines their properties—a biophysical characterization
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Protein Science. 2021;
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IF = 6.725
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Santo Lentini; D. - Petrvalská; Olivia - Obšilová; Veronika - Ottmann; Ch. - Obšil; Tomáš
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Stabilization of Protein-Protein Interactions between CaMKK2 and 14-3-3 by Fusicoccins
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ACS Chemical Biology. 2020; 15(11); 3060-3071
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IF = 5.100
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Pšenáková; Katarína - Hexnerová; Rozálie - Srb; Pavel - Obšilová; Veronika - Veverka; Václav - Obšil; Tomáš
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The redox-active site of thioredoxin is directly involved in apoptosis signal-regulating kinase 1 binding that is modulated by oxidative stress
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FEBS Journal. 2020; 287(8); 1626); 1644
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IF = 5.542
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Obšilová; Veronika - Obšil; Tomáš
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The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
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International Journal of Molecular Sciences. 2020; 21(22)); 8824
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IF = 5.923
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Detailed insight on structure of the complex 14-3-3:Nth1 (PDB 5M4A). Alblova et al. (2017).
A) Identification of key phosphorylation sites responsible for 14-3-3-dependent activation of neutral trehalase Nth1. B) Decrease of H/D kinetics for a peptide in Ca-binding domain which lies on the interface between the two proteins induced by Bmh1. C) SAXS low resolution structure of the Nth1:Bmh1 complex. Veisova et al. (2012), Macakova et al. (2013), Kopecka et al. (2014).
Protein 14-3-3 interacts with N- and C-termini of Gtβγ binding interfaces of phosducinu. Kacirova et al. (2015).
