RNDr. Veronika Obšilová, Ph.D.

RNDr. Veronika Obšilová, Ph.D.

The Institute of Physiology of the Czech Academy of Sciences
Head of Group Structural biology of signaling proteins

veronika.obsilova@fgu.cas.cz
+420325873513, +420325873507

She leads the Laboratory of structural biology of signaling protiens at the Institute of Physiology, CAS, which focuses 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 proteinkinases 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

For more information please visit: Structural Biology of Signaling Proteins - Institute of Physiology AS CR, v.v.i. (cas.cz)

Veronika Obšilová in Pubmed

Recent publications

2024

Honzejkova K, Kosek D, Obsilova V, Obsil T. (2024) The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1. Elife 13:RP95199. DOI: 10.7554/eLife.95199.

Obsilova V, Obsil T. (2024) The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways. Front Mol Biosci. 24:1327014. DOI: 10.3389/fmolb.2024.1327014.

2023

Petrvalska O, Honzejkova K, Koupilova N, Herman P, Obsilova V, Obsil T. (2023) 14-3-3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C-terminal helices. Protein Sci. 32:e4805. DOI: 10.1002/pro.4805.

Masaryk J, Kale D, Pohl P, Ruiz-Castilla FJ, Zimmermannová O, Obšilová V, Ramos J, Sychrová H. (2023) The second intracellular loop of the yeast Trk1 potassium transporter is involved in regulation of activity, and interaction with 14-3-3 proteins. Comput Struct Biotechnol J. 21:2705-2716. DOI: 10.1016/j.csbj.2023.04.019.

2022

Kohoutova K, Docekal V, Ausserlechner MJ, Kaiser N, Tekel A, Mandal R, Horvath M, Obsilova V, Vesely J, Hagenbuchner J and Obsil T (2022) Lengthening the Guanidine−Aryl Linker of Phenylpyrimidinylguanidines Increases Their Potency as Inhibitors of FOXO3-Induced Gene Transcription. ACS Omega 7(38):34632-34646. DOI: 10.1021/acsomega.2c04613.

Obsilova V and Obsil T (2022) Structural insights into the functional roles of 14-3-3 proteins. Front. Mol. Biosci. 9:1016071. DOI: 10.3389/fmolb.2022.1016071.

Joshi R, Pohl P, Strachotova D, Herman P, Obsil T, Obsilova V. (2022) Nedd4-2 binding to 14-3-3 modulates the accessibility of its catalytic site and WW domains. Biophys. J. 121(7):1299-1311. DOI: 10.1016/j.bpj.2022.02.025.

Mandal R, Kohoutova K, Petrvalska O, Horvath M, Srb P, Veverka V, Obsilova V and Obsil T (2022) FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA. Protein Sci. 31:e4287. DOI: 10.1002/pro.4287

2021

Pohl P, Joshi R, Petrvalska O, Obsil T and Obsilova V. (2021) 14-3-3-protein regulates Nedd4-2 by modulating interactions between HECT and WW domains. Commun. Biol. 4(1):899. DOI: 10.1038/s42003-021-02419-0

Horvath M, Petrvalska O, Herman P, Obsilova V and Obsil T. (2021) 14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites. Commun. Biol. 4(1):986. DOI: 10.1038/s42003-021-02518-y

Obsilova V, Honzejkova K and Obsil T. (2021) Structural Insights Support Targeting ASK1 Kinase for Therapeutic Interventions. Int. J. Mol. Sci. 22(24):13395. DOI:10.3390/ijms222413395.

2020

Kalabova D, Filandr F, Alblova M, Petrvalska O, Horvath M, Man P, Obsil T, Obsilova V. (2020) 14-3-3 protein binding blocks the dimerization interface of caspase-2. FEBS J. 287(16):3494-3510. DOI: 10.1111/febs.15215

Psenakova K, Hexnerova R, Srb P, Obsilova V, Veverka V, Obsil T. (2020) The redox active site of thioredoxin is directly involved in apoptosis signal-regulating kinase 1 binding that is modulated by oxidative stress. FEBS J. 287(8):1626-1644. DOI: 10.1111/febs.15101

Obsilova V and Obsil T. (2020) The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases. Int. J. Mol. Sci. 21(22):8824. DOI: 10.3390/ijms21228824

Obsilova V and Obsil T. (2020) A new role for 14-3-3 protein in steroidogenesis. FEBS J. 287(18):3921-3924. DOI: 10.1111/febs.15507

2019

Alblova M, Smidova A, Kalabova D, Lentini Santo D, Obsil T, Obsilova V. (2019) Allosteric activation of yeast enzyme neutral trehalase by calcium and 14-3-3 protein.
Physiol Res. (2019) 68(2):147-160. DOI: 10.33549/physiolres.933950

Hagenbuchner J, Obsilova V, Kaserer T, Kaiser N, Rass B, Psenakova K, Docekal V, Alblova M, Kohoutova K, Schuster D, Aneichyk T, Vesely J, Obexer P, Obsil T, Ausserlechner MJ. (2019) Modulating FOXO3 transcriptional activity by small, DBD-binding molecules. Elife. 8. pii: e48876. DOI: 10.7554/eLife.48876

Psenakova K, Kohoutova K, Obsilova V, Ausserlechner MJ, Veverka V, Obsil T. (2019) Forkhead Domains of FOXO Transcription Factors Differ in both Overall Conformation and Dynamics. Cells. 8(9). pii: E966. DOI: 10.3390/cells8090966

Alblova M, Smidova A, Kalabova D, Lentini Santo D, Obsil T, Obsilova V. Allosteric activation of yeast enzyme neutral trehalase by calcium and 14-3-3 protein. Physiol Res. 2019 Apr 30;68(2):147-160. DOI: 10.33549/physiolres.933950

Smidova A, Stankova K, Petrvalska O, Lazar J, Sychrova H, Obsil T, Zimmermannova O, Obsilova V. (2019) The activity of Saccharomyces cerevisiae Na+, K+/H+ antiporter Nha1 is negatively regulated by 14-3-3 protein binding at serine 481. Biochim Biophys Acta Mol Cell Res. 1866(12):118534. DOI: 10.1016/j.bbamcr.2019.118534

2018

Smidova A, Alblova M, Kalabova D, Psenakova K, Rosulek M, Herman P, Obsil T, Obsilova V. (2018) 14-3-3 protein masks the nuclear localization sequence of caspase-2. FEBS J. (2018) 285(22):4196-4213. DOI: 10.1111/febs.14670

Kylarova S, Psenakova K, Herman P, Obsilova V, Obsil T. (2018) CaMKK2 kinase domain interacts with the autoinhibitory region through the N-terminal lobe including the RP insert. Biochim. Biophys. Acta-Gen. Subj. 1862(10):2304-2313. DOI: 10.1016/j.bbagen.2018.07.025

Psenakova K, Petrvalska O, Kylarova S, Lentini Santo D, Kalabova D, Herman P, Obsilova V, Obsil T. (2018) 14-3-3 protein directly interacts with the kinase domain of calcium/calmodulin-dependent protein kinase kinase (CaMKK2). Biochim. Biophys. Acta-Gen. Subj. 1862(7):1612-1625. DOI: 10.1016/j.bbagen.2018.04.006

2017

Alblova M, Smidova A, Docekal V, Vesely J, Herman P, Obsilova V, Obsil T. Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1. Proc Natl Acad Sci U S A. 2017, 114:E9811-E9820.

Kalabova D, Smidova A, Petrvalska O, Alblova M, Kosek D, Man P, Obsil T, Obsilova V. Human procaspase-2 phosphorylation at both S139 and S164 is required for 14-3-3 binding. Biochem Biophys Res Commun. 2017, 493:940-945.

Kacirova M, Novacek J, Man P, Obsilova V, Obsil T. Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function. Biophys J. 2017, 112:1339-1349.

2016

Kylarova S, Kosek D, Petrvalska O, Psenakova K, Man P, Vecer J, Herman P, Obsilova V, Obsil T. Cysteine residues mediate high-affinity binding of thioredoxin to ASK1. FEBS J. 2016, 283:3821-3838.

Petrvalska O, Kosek D, Kukacka Z, Tosner Z, Man P, Vecer J, Herman P, Obsilova V, Obsil T. Structural Insight into the 14-3-3 Protein-dependent Inhibition of Protein Kinase ASK1 (Apoptosis Signal-regulating kinase 1). J Biol Chem. 2016, 291:20753-65.

2015

Kacirova M, Kosek D, Kadek A, Man P, Vecer J, Herman P, Obsilova V, Obsil T. Structural Characterization of Phosducin and Its Complex with the 14-3-3 Protein. J Biol Chem. 2015, 290:16246-60.

2014

Kosek D, Kylarova S, Psenakova K, Rezabkova L, Herman P, Vecer J, Obsilova V, Obsil T. Biophysical and structural characterization of the thioredoxin-binding domain of protein kinase ASK1 and its interaction with reduced thioredoxin. J Biol Chem. 2014, 289:24463-74.

Kopecka M, Kosek D, Kukacka Z, Rezabkova L, Man P, Novak P, Obsil T, Obsilova V. Role of the EF-hand-like motif in the 14-3-3 protein-mediated activation of yeast neutral trehalase Nth1. J Biol Chem. 2014, 289:13948-61.

2013

Macakova E, Kopecka M, Kukacka Z, Veisova D, Novak P, Man P, Obsil T, Obsilova V. Structural basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1. Biochim Biophys Acta. 2013, 1830:4491-9.

2012

Veisova D, Macakova E, Rezabkova L, Sulc M, Vacha P, Sychrova H, Obsil T, Obsilova V. Role of individual phosphorylation sites for the 14-3-3-protein-dependent activation of yeast neutral trehalase Nth1. Biochem J. 2012,443:663-670.