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Our group 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 by 14-3-3 protein
- Study of DNA-binding domain of transcription factor FOXO4
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
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Kopecka M, Kosek D, Kukacka Z, Rezabkova L, Man P, Novak P, Obsil T, Obsilova V.
J Biol Chem. 2014 May 16;289(20):13948-61.
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Publications
Šmídová, Aneta - Alblová, Miroslava - Kalábová, Dana - Pšenáková, Katarína - Rosůlek, Michal - Herman, P. - Obšil, Tomáš - Obšilová, Veronika
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14-3-3 protein masks the nuclear localization sequence of caspase-2
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FEBS Journal 2018, 285(22), 4196-4213
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IF = 4.530
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Pšenáková, Katarína - Petrvalská, Olivia - Kylarová, Salome - Santo, D. L. - Kalábová, Dana - Herman, P. - Obšilová, Veronika - Obšil, Tomáš
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14-3-3 protein directly interacts with the kinase domain of calcium/calmodulin-dependent protein kinase kinase (CaMKK2)
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Biochimica et Biophysica Acta. General Subjects 2018, roč. 1862, 7, p. 1612-1625
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IF = 3.679
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doi
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Kylarová, Salome - Pšenáková, Katarína - Herman, P. - Obšilová, Veronika - Obšil, Tomáš
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CaMKK2 kinase domain interacts with the autoinhibitory region through the N-terminal lobe including the RP insert
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Biochimica et Biophysica Acta. General Subjects 2018, 1862(10), 2304-2313
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IF = 3.679
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doi
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Kalábová, Dana - Šmídová, Aneta - Petrvalská, Olivia - Alblová, Miroslava - Košek, Dalibor - Man, Petr - Obšil, Tomáš - Obšilová, Veronika
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Human procaspase-2 phosphorylation at both S139 and S164 is required for 14-3-3 binding
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Biochemical and Biophysical Research Communications. 2017, roč. 493, 2, p. 940-945
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IF = 2.559
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Kacířová, Miroslava - Nováček, J. - Man, Petr - Obšilová, Veronika - Obšil, Tomáš
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Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function
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Biophysical Journal. 2017, roč. 112, 7, p. 1339-1349
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IF = 3.495
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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).
