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Notch pathway plays a critical role during the development and life of metazoan organisms. CSL proteins are the component of the Notch pathway that mediates the regulation of target genes. The discovery of CSL-like proteins in yeast raised the question of their function in unicellular organisms which did not utilize the canonical Notch pathway. CSL-homologues in yeast are conserved in parts that are important for DNA binding and for fission yeast proteins it was shown that they bind to CSL recognition elements in vitro. In fission yeast, CSL paralogues Cbf11 and Cbf12 play antagonistic roles in cell adhesion and the coordination of cell and nuclear division. Yeast CSL proteins have long and intrinsically unstructured N- terminal domains compared to metazoan CSL proteins. In this study, we investigated the functional significance of these extended N-termini of CSL proteins by their complete removal. For newly constructed truncated variants of proteins Cbf11 and Cbf12 in Schizosaccharomyces pombe we observed the lack of ability to bind CSL recognition RBP probe. The removal of N-terminal parts of CSL proteins in fission yeast led to the change in their cellular localization. Once strongly preferred nuclear localization changed by the removal of N-terminal domains to cytoplasmic localization with a...

Interactome of IL-1α N-terminal domain Cytokines are highly effective mediators produced by various cell types within and outside of the immune system with the aim to influence the orientation, intensity, and duration of the immune response and inflammatory process. Their biological effects mediated through binding the high-affinity membrane receptors and triggering the signal transduction pathway are usually well defined. However, as it is more and more frequently observed, in addition to the exocrine function, some cytokines may show intracrine effects. For this type of cytokines, the term "dual function cytokines" has been adopted. One of these cytokines is Interleukin-1α, in which the recent research has concentrated on determining its intracellular functions. The intracellular function of interleukin-1α has not been clearly defined so far. However, apart from the absence of the conventional hydrophobic sequence, its existence is supported by the fact that the N-terminal peptide included in its precursor is highly conserved and contains nuclear localization signal. The aim of this work is to define the conditions of localization of the interleukin-1α N- terminal domain in different cellular compartments and to study proteins potentially interacting with it using fluorescent microscopy. Key words:...