Laboratory of Calcium Binding Proteins
Head: Anna FILIPEK
Staff: Agnieszka Graczyk (PhD student), Ewelina Jurewicz, Ewa Kilańczyk, Jacek Kuźnicki, Wiesława Leśniak, Wiktor Prus (PhD student), Agnieszka Góral (PhD student), Agnieszka Topolska (PhD student), Urszula Wasik (PhD student)
Research profile:
The laboratory is focused on studying the regulation of calcium homeostasis and its impact on processes related to cell proliferation and differentiation. In particular, our group studies the role of the calcium binding protein, S100A6, and its ligands: Sgt1, CacyBP/SIP and p53 in cellular signaling pathways especially those involving the ERK1/2 kinases. We also investigate the involvement of complexes formed by S100A6 and its ligands in ubiquitination, cytoskeletal organization and cellular response to stress under normal and pathological conditions. In addition, we study the transcriptional and epigenetic regulation of genes encoding S100A6, Sgt1 and CacyBP/SIP as well as posttranslational modifications of these proteins in relation to their function.
Methods:
• cell culture and transfection
• plasmid construction
• immunocyto/histochemistry
• Western blot
• chemical cross-linking
• co-immunoprecipitation
• luciferase assay
• gel-shift
• chromatin immunoprecipitation (ChIP)
• bisulfite DNA modification
Current research activities:
• studies of the Sgt1 function in nucleus under stress conditions
• studies of the role of S100A6, CacyBP/SIP and ERK1/2 in cell proliferation and differentiation
• studies of the role of CacyBP/SIP in neuronal cytoskeleton dynamics through interaction with tubulin and actin
• studies of the S100A6-p53 interaction and its impact on cell physiology
• studies of the posttranslational modifications of CacyBP/ SIP, Sgt1 and p53
• studies of the transcriptional and epigenetic regulation of gene expression
Selected publications:
Prus W., Żabka M., Bieganowski P., Filipek A. (2011) Nuclear translocation of Sgt1 depends on its phosphorylation state. The International Journal of Biochemistry and Cell Biology, 43:1747-1753.
Kilańczyk E., Filipek S., Filipek A. (2011) ERK1/2 is dephosphorylated by a novel phosphatase – CacyBP/SIP. Biochemical and Biophysical Research Communications, 404:179-183.
Słomnicki L.P., Leśniak W. (2010) S100A6 (calcyclin) induces senescence-like changes in cell cycle, morphology and functional characteristics of mouse NIH 3T3 fibroblasts. Journal of Cellular Biochemistry, 109: 576-584.
Schneider G., Nieznański K., Jóźwiak J., Słomnicki L.P., Rędowicz M.J., Filipek A. (2010) Tubulin binding protein, CacyBP/SIP, induces actin polymerization and may link actin and tubulin cytoskeletons. Biochimica et Biophysica Acta, 1803: 1308–1317.
Słomnicki Ł.P., Nawrot B., Leśniak W. (2009) S100A6 binds p53 and affects its activity. International Journal of Biochemistry and Cell Biology, 41: 784-790.
