Department of Cell Biology
Head: Dr. Sc. Katarzyna Kwiatkowska
The Department of Cell Biology consists of research groups whose common interests address fundamental issues of plasma membrane receptor activation and signal transduction under physiological and pathological conditions. Approaches range from molecular biology to whole-organism physiology.
Endocytosis and degradative pathways in a variety of different cell types undergoing gene silencing (RNAi) and stimulation are investigated by the group led by Prof. Wyroba. The products encoded by the genes cloned in this laboratory in a model unicellular eukaryote Paramecium octaurelia, indispensable for endosome/phagosome formation, sorting and membrane trafficking including Rab7 and its effectors, are characterized.
Cytoskeletal proteins and cytoskeleton reorganization, particularly actin and tubulin, in protists and mammalian cells and their role in physiological cell responses are the research themes of Prof. Fabczak’s group. In addition, studies on the structure and function of mechanosensitive channels from Escherichia coli membrane are carried out.
Immunoresponses and their underlying mechanisms, such as TLR4 signalling on macrophages, are investigated by Prof. Kwiatkowska’s group. The essential approach is to examine how activated receptors initiate cascades of events leading to pro-inflammatory responses of cells. In particular, this group focuses on the involvement of lipids and proteins enriched in rafts of the plasma membrane in receptor signalling, including the role of PIP2, phosphoinositide and tyrosine kinases, sphingomyelin and its derivatives in modu- lation of cytokine production, particle internalization and submembrane cytoskeleton reorganization.
Grainyhead-like (GRHL) transcription factors in signal transduction in mammalian cells are investigated by Dr. Wilanowski’s group. These studies aim to unravel the mechanisms of GRHL functions in health and disease, and the roles of the GRHL factors in skin cancer and in wound healing.
Neuromuscular junctions (NMJs) and their maturation mechanisms are investigated by Dr. Prószyński’s group. The goal of their research is to elucidate, in detail, the function of candidate postsynaptic organizers, search for novel key regulators and explore possibility that podosomes, actin- rich, dynamic, adhesive organelles may be involved in this process.
Bregier C., Krzemień-Ojak L., Włoga D., Jerka-Dziadosz M., Joachimiak E., Batko K., Filipiuk I., Smietanka U., Gaertig J., Fabczak S., Fabczak H. (2013) PHLP2 is essential and plays a role in ciliogenesis and microtubule assembly in Tetrahymena thermophila. Journal of Cellular Physiology, 228: 2175-2189.
Prószyński T.J., Sanes J.R. (2013) Amotl2 interacts with LL5β, localizes to podosomes and regulates postsynaptic differentiation in muscle. Journal of Cell Science, 126: 2225-2235.
Kleveta G., Borzęcka K., Zdioruk M.I., Czerkies M., Kuberczyk H., Sybirna N., Sobota A., Kwiatkowska K. (2012) LPS induces phosphorylation of actin-regulatory proteins leading to actin reassembly and macrophage motility. Journal of Cellular Biochemistry, 113: 80-92.
Liu L., Wyroba E., Satir B.H. (2011) RNAi knockdown of parafusin inhibits the secretory pathway. European Journal of Cell Biology, 90: 844-853.
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.
Darido C., Georgy S.R., Wilanowski T., Dworkin S., Auden A., Zhao Q., Rank G., Srivastava S., Finlay M.J., Papenfuss A.T., Pandolfi P.P., Pearson R.B., Jane S.M. (2011) Targeting of the tumor suppressor GRHL3 by a miR-21-dependent proto-oncogenic network results in PTEN loss and tumorigenesis. Cancer Cell 20: 635-648.
Józefowski S., Czerkies M., Łukasik A., Bielawska A., Bielawski J., Kwiatkowska K., Sobota A. (2010) Ceramide and ceramide 1-phosphate are negative regulators of TNF-a production induced by lipopolysaccharide. Journal of Immunology, 185: 6960-6973.
Kulma M., Hereć M., Grudziński W., Anderluh G., Gruszecki W.I., Kwiatkowska K., Sobota A. (2010) Sphingomyelin-rich domains are sites of lysenin oligomerization: implications for raft studies. Biochimica et Biophysica Acta, 1798: 471-481.
Włoga D., Dave D., Meagley J., Rogowski K., Jerka-Dziadosz M., Gaertig J. (2010) Hyperglutamylation of tubulin can either tabilize or destabilize microtubules in the same cell. Eukaryotic Cell. 9: 184-193.