Proteosynthesis and proteostasis group
     Laboratory of Cell Signalling


      Institute of Microbiology


Czech Academy of Sciences


Group members:

Tomáš Groušl  - group leader
(ORCID: 0000-0002-6996-1323)

Věra Chvalová - PhD student
(ORCID: 0009-0001-2321-3098)

Vignesh Venkadasubramanian - PhD student
(ORCID: 0000-0003-1700-7439)

Kateřina Rollerová - Master student


Alumni:

                     Marina Sokol (2020-2023)


Summer school:

                  Veronika Lišková (UCT Prague)


Collaborators:

                    Aleš Vančura - Laboratory of Epigenetics (St. John's College of Liberal Arts and Science)

                    Axel Mogk - Biogenesis & quality control of proteins (Zentrum für Molekulare Biologie der Universität Heidelberg)

                    Ayala Shiber - Faculty of Biology (Technion - Israel Institute of Technology)

                    Jana Vojtová - Laboratory of Regulation of Gene Expression (Inst. of Microbiology of the Czech Academy of Sciences)

                    Mark Rinnerthaler - Genetics and Biology of Aging (Paris Lodron University Salzburg)

                    Christof Taxis - Faculty of Medicine (Health and Medical University Erfurt)

                    Olga Zimmermannová - Laboratory of Membrane Transport (Inst. of Physiology of the Czech Academy of Sciences)


Publications in preparation:

Venkadasubramanian V., Chvalova V., Sokolova M., Rasl J., Grusanovic J., Marvalova O., Vomastek T., Grousl T.:
Elucidating the role and the position of RACK1 in stress granules by its ribosome binding-deficient and glycosylation-deficient mutants

Grousl T.,Vojtova J.,Vomastek T.:
Revealing the assemblies of yeast stress granules and Processing bodies by expansion and super-resolution microscopy

Grousl T.,Vojtova J.,Vomastek T.:
Xrn1 associates with eisosomal complexes independently on its sequestration in P-bodies

Grousl T., Vomastek T.:
Yeast P-bodies at a glance.


Publications under review:



Publications of the group members:

Vojtova J., Capek M., Willeit S., Grousl T., Chvalova V., Valasek L.S., Kutejova E., Pevala V., Rinnerthaler M.:
A fully automated morphological analysis of yeast mitochondria from wide-field fluorescence images
Scientific Reports.
2024 Dec 3;14(1):30144. doi: 10.1038/s41598-024-81241-0.

Zmuda M., Sedlackova E., Pravdova B., Cizkova M., Cerny O., Allsop T., Grousl T., Malcova I., Kamanova J.:
The Bordetella effector protein BteA induces host cell death by disruption of calcium homeostasis
mBio,
2024 Dec 11;15(12):e0192524. doi: 10.1128/mbio.01925-24.

Rasl J., Caslavsky J., Grusanovic J., Chvalova V., Kosla J., Adamec J., Grousl T., Klimova Z., Vomastek T.:
Depletion of calpain2 accelerates epithelial barrier establishment and reduces growth factor-induced cell scattering
Cell Signal. 2024 Sep;121:111295. doi: 10.1016/j.cellsig.2024.111295. Epub 2024 Jul 10.

Grousl T., Vomastek T. (2024):
Xrn1 exoribonuclease – an intrinsic marker of yeast population growth
Front. Biosci. (Elite Ed) 2024, 16(1), 1; https://doi.org/10.31083/j.fbe1601001

Chvalova V., Vomastek T., Grousl T. (2024):
Comparison of holotomographic microscopy and coherence-controlled holographic microscopy
Journal of Microscopy, 1–9. https://doi.org/10.1111/jmi.13260

Chvalova V.; Venkadasubramanian V.; Klimova Z.; Vojtova J.; Benada O.; Vanatko O.; Vomastek T.; Grousl T. (2023):
Characterization of RACK1-depleted mammalian cells by a palette of microscopy approaches reveals defects in cell cycle progression and polarity establishment
Exp Cell Res. 2023 (430) 113695. doi.org/10.1016/j.yexcr.2023.113695

Jawed A., Ho Ch.T., Grousl T., Shrivastava A., Ruppert T., Bukau B., Mogk A. (2023):
Balanced activities of Hsp70 and the ubiquitin proteasome system underlie cellular protein homeostasis
Front Mol Biosci. 2023 Jan 4;9:1106477. doi: 10.3389/fmolb.2022.1106477.

Rasl J., Grusanovic J., Klímová Z., Caslavsky J., Grousl T., Novotny J., Kolar M., Vomastek T. (2022):
ERK2 signaling regulates cell-cell adhesion of epithelial cells and enhances growth factor-induced cell scattering

Cell Signal. 2022 Nov;99:110431. doi: 10.1016/j.cellsig.2022.110431.

Grousl T.#, Vojtova J., Hasek J., Vomastek T. (2021):
Yeast stress granules at a glance.

Yeast. 2021. doi: 10.1002/yea.3681.
# Corresponding author

Ramaniuk O., Klimova Z., Grousl T.#, Vomastek T.# (2020):
Quantitative Phase Imaging of Spreading Fibroblasts Identifies the Role of Focal Adhesion Kinase in the Stabilization of the Cell Rear.

Biomolecules. 2020. doi: 10.3390/biom10081089.
# Corresponding authors

Ho Ch.T., Grousl T., Shatz O., Jawed A., Ruger-Herreros C., Semmelink M., Zahn R., Richter K., Bukau B., Mogk M. (2019):
Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis.

Nat Commun. 2019. doi: 10.1038/s41467-019-12868-1.

Grousl T.*, Ungelenk S.*, Miller S.*, Ho Ch.T., Khokhrina M., Mayer M.P., Bukau B., Mogk A. (2018):
A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins.

J Cell Biol. 2018 Jan 23 pii: jcb.201708116
* These authors contributed equally to this work.

Ungelenk S., Moayed F., Ho Ch.T., Grousl T., Scharf A., Mashaghi A., Tans S., Mayer M.P., Mogk A. & Bukau B. (2016):
Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding.

Nature Commun., 2016 Nov 30;7:13673. doi: 10.1038/ncomms13673.

Poornima G., Shah S., Vignesh V., Parker R., Rajyaguru P.I. (2016):
Arginine methylation promotes translation repression activity of eIF4G-binding protein, Scd6
Nucleic Acids Res. 2016 Nov 2;44(19):9358-9368. doi: 10.1093/nar/gkw762

Cherkasov V.*, Grousl T.*, Theer P., Vainshtein Y., Glaßer C., Mongis C., Kramer G., Stoecklin G., Knop M., Mogk A.,
Bukau B.(2015):
Systemic control of protein synthesis through coordinated sequestration of translation and ribosome biogenesis factors during severe heat stress.

FEBS Lett. 2015 Nov 30;589(23):3654-64. doi: 10.1016/j.febslet.2015.10.010.
* These authors contributed equally to this work.

Grousl T.*, Opekarova M.*, Stradalova V., Hasek J., Malinsky J. (2015):
Evolutionarily conserved 5'-3' exoribonuclease Xrn1 accumulates at plasma membrane-associated eisosomes in post-diauxic yeast.

PLoS One. 2015 Mar 26;10(3):e0122770. doi: 10.1371/journal.pone.0122770.
*
These authors contributed equally to this work.

Rinnerthaler M., Lejskova R., Grousl T., Stradalova V., Heeren G., Richter K., Breitenbach-Koller L., Malinsky J., Hasek J., Breitenbach M. (2013):
Mmi1, the Yeast Homologue of Mammalian TCTP, Associates with Stress Granules in Heat-Shocked Cells and Modulates Proteasome Activity.

PLoS ONE 8 (10). doi:10.1371/journal.pone.0077791.

Grousl T., Ivanov P., Malcova I., Pompach P., Frydlova I., Slaba R., Senohrabkova L., Novakova L., Hasek J. (2013):
Heat Shock-Induced Accumulation of Translation Elongation and Termination Factors Precedes Assembly of Stress Granules in S. Cerevisiae.

PLoS ONE 8 (2). doi:10.1371/journal.pone.0057083.

Rinnerthaler M., Buttner S., Laun P., Heeren G., Felder T.K., Klinger H., Weinberger M., Stolze K., Grousl T., Hasek J., Benada O., Frydlova I., Klocker A., Simon-Nobbe B., Jansko B., Breitenbach-Koller H., Eisenberg T., Gourlay C.W., Madeo F., Burhans W.C., Breitenbach M. (2012):
Yno1p/Aim14p, a NADPH-oxidase ortholog, controls extramitochondrial reactive oxygen species generation, apoptosis, and actin cable formation in yeast.

Proc Natl Acad Sci USA. 2012 May 29;109(22):8658-63. doi: 10.1073/pnas.1201629109.

Grousl T., Ivanov P., Frydlova I., Vasicova P., Janda F., Vojtova J., Malinska K., Malcova I., Novakova L., Janoskova D., Valasek L., Hasek J. (2009):
Robust Heat Shock Induces eIF2alpha-Phosphorylation-Independent Assembly of Stress Granules Containing eIF3 and 40S Ribosomal Subunits in Budding Yeast, Saccharomyces Cerevisiae.

Journal of Cell Science 122 (Pt 12): 2078-88. doi:10.1242/jcs.045104.

Prevorovsky M., Grousl T., Stanurova J., Rynes J., Nellen W., Puta F., Folk P. (2009):
Cbf11 and Cbf12, the Fission Yeast CSL Proteins, Play Opposing Roles in Cell Adhesion and Coordination of Cell and Nuclear Division.

Experimental Cell Research 315 (8): 1533-47. doi:10.1016/j.yexcr.2008.12.001.

Funding provided:

      
Czech Science Foundation



      Charles University Grant Agency

           
Czech BioImaging


     Czech Infrastructure for    
     Integrative Structural Biology

     Czech Academy of Sciences

Partners:


Biocev



Česko-slovenská biologická společnost


Telight company