Kvido Stříšovský Group

About our group

The research in Strisovsky lab is focused on biological membranes and enzymatic catalysis occurring in their context. We are studying the ubiquitous intramembrane proteases of the rhomboid family and the mechanistic aspects of their functions relevant for biological signaling, membrane protein biogenesis and homeostasis. In our work we integrate the tools of membrane biochemistry, enzymology and structural biology to understand how rhomboid proteases recognise and select substrates, and employ methods of quantitative proteomics, cell biology and genetics to uncover molecular basis of rhomboid functions in organisms. We are an international group and we are always eager to consider motivated students and postdocs who would like to join us. If interested, contact Kvido Strisovsky.

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31 December 2021

A temporary farewell

Alma, Hanka and Šárka are taking a sabbatical from the group to devote their time to an enriching activity that each of us have participated in in some form at least once. We are looking forward to having you back at some point!

31 December 2021

Anežka leaves the group.

Anežka Tichá leaves the group after seven great years as a PhD student and postdoc. We are sad to see you go and wish you all the best in your new position!

18 December 2021

new paper from the group

We have contributed to a collaborative paper on the EMC complex with the Adrain, Domingos and Christianson groups that has just been published in the EMBO Reports.

3 December 2021

new paper from the group

We have contributed to a collaborative paper with the Freeman lab that explores the role of the human rhomboid intramembrane protease RHBDL2. Just coming out in Molecular Cell.

Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease

J. Began B. Cordier J. Březinová J. Delisle R. Hexnerová P. Srb P. Rampírová M. Kožíšek M. Baudet J. Couté A. Galinier V. Veverka T. Doan K. Stříšovský

EMBO Journal 39 (10): e102935 (2020)

Magnesium homeostasis is essential for life and depends on magnesium transporters, whose activity and ion selectivity need to be tightly controlled. Rhomboid intramembrane proteases pervade the prokaryotic kingdom, but their functions are largely elusive. Using proteomics, we find that Bacillus subtilis rhomboid protease YqgP interacts with the membrane‐bound ATP‐dependent processive metalloprotease FtsH and cleaves MgtE, the major high‐affinity magnesium transporter in B. subtilis. MgtE cleavage by YqgP is potentiated in conditions of low magnesium and high manganese or zinc, thereby protecting B. subtilis from Mn²⁺/Zn²⁺ toxicity. The N‐terminal cytosolic domain of YqgP binds Mn²⁺ and Zn²⁺ ions and facilitates MgtE cleavage. Independently of its intrinsic protease activity, YqgP acts as a substrate adaptor for FtsH, a function that is necessary for degradation of MgtE. YqgP thus unites protease and pseudoprotease function, hinting at the evolutionary origin of rhomboid…

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Maintenance of organellar protein homeostasis by ER-associated degradation and related mechanisms

M. K. Lemberg K. Stříšovský

Molecular Cell 81 (12): 2507-2519 (2021)

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The Rhomboid Superfamily: Structural Mechanisms and Chemical Biology Opportunities

A. Tichá B. Collis K. Stříšovský

Trends in Biochemical Sciences 43 (9): 726-739 (2018)

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General and Modular Strategy for Designing Potent, Selective, and Pharmacologically Compliant Inhibitors of Rhomboid Proteases

A. Tichá S. Stanchev K. R. Vinothkumar D. C. Mikles P. Pachl J. Began J. Škerle K. Švehlová M. T. N. Nguyen S. H. L. Verhelst D. C. Johnson D. A. Bachovchin M. Lepšík P. Majer K. Stříšovský

Cell Chemical Biology 24 (12): 1523-1536 (2017)

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Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate-peptide complex structures

S. Zoll S. Stanchev J. Began J. Škerle M. Lepšík L. Peclinovská P. Majer K. Stříšovský

EMBO Journal 33 (20): 2408-2421 (2014)

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