Laboratory of Physiology of Cell Movements
Head: Stanisław FABCZAK
Staff: Cezary Bregier, Hanna Fabczak, Maria Jerka-Dziadosz (Professor emeritus), Ewa Joachimiak, Piotr Koprowski, Łucja Krzemień-Ojak (PhD student), Andrzej Kubalski, Leszek Kuźnicki (Professor emeritus), Urszula Śmietanka, Ewa Wacławek (PhD student), Paulina Urbańska, Anna Wasik, Dorota Włoga
Research profile:
We investigate the mechanisms which affect the cell cyto- skeleton assembly and its reorganization. Currently, we study the function of phosducin-like proteins (PhLPs) involved in folding of cytoskeletal proteins, particularly actin and tubulin, in protists and mammalian cells. Properly folded tubulin is essential to maintain the correct structure and function of microtubules. Cilia, the microtubules based cell extensions, are conserved organelles that play a key role in the cell motility and signal transduction. Dysfunction of cilia causes a number of human disorders known as ciliopathies. We carry out proteomic and functional analysis of the proteins involved in the ciliogenesis in protozoan cells and immortalized mammalian cell lines. Another major project concentrates on the role of extracellular factors in the dynamics of actin cytoskeleton in Amoeba proteus and on the identification and determination of the function of actin binding proteins. We also investigate the structure and func- tion of mechanosensitive ion channels in Escherichia coli
Methods:
• fluorescence resonance energy transfer (FRET) analysis
• molecular biology and genetic engineering techniques
• patch-clamp techniques
• standard biochemical and immunocytochemical methods
• ultrastructure analysis at the electron and scanning microscopy levels
Current research activities:
• determination of the effect of PhLPs genes konockout on microtubules assembly and cilia ultrastructure and function
• analysis of the PhLPs function as a modulator of chaperonin CCT during tubulin and actin folding in mammalian cell lines
• proteomic and functional analysis of proteins involved in ciliogenesis in protozoan cells and immortalized mammalian cell lines
• identification of actin binding proteins responsible for actin cytoskeleton reorganization in Amoeba proteus
• patch-clamp studies on mechanosensitive ion channels from the cytoplasmic membrane of Escherichia coli and investigation of the role of their C-termini in the channel gating
Selected publications:
Koprowski P., Grajkowski W., Isacoff E.Y., Kubalski A. (2011) Genetic screen for potassium leaky small mechanosensitive channels (MscS) in E. coli: recognition of cytoplasmic beta domain as a new gating element. Journal of Biological Chemistry, 286: 877-888.
Sobierajska K., Joachimiak E., Bregier C., Fabczak S., Fabczak H. (2011) Effect of phosducin silencing on the photokinetic motile response of Blepharisma japonicum. Photochemical and Photobiological Sciences, 10: 19-24.
Włoga D., Dave D., Meagley J., Rogowski K., Jerka-Dziadosz M., Gaertig J. (2010) Hyperglutamylation of tubulin can either stabilise or destabilise microtubules in the same cell. Eukaryotic Cell, 9: 184 -193.
Sobierajska K., Głos J., Dąborowska J., Kucharska J., Bregier C., Fabczak S., Fabczak H. (2010) Visualisation of the interaction between Gβγ and tubulin during light-induced cell elongation of Blepharisma japonicum. Photochemical and Photobiological Sciences, 9: 1101-1110.
Włoga D., Webster D.M., Rogowski K., Bre M. H., Levilliers N., Jerka-Dziadosz M., Janke C., Dougan S.T., Gaertig J. (2009) TTLL3 is a tubulin glycine ligase that regulates the assembly of cilia. Developmental Cell, 16: 867-876.
