Tag Archives: Ruk/CIN85

Scientific and practical activity of the Laboratory of Cell Signaling Mechanisms of the Palladin Institute of Biochemistry of NAS of Ukraine

R. P. Vynogradova, I. Yu. Chernysh, V. M. Danilova

Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: valdan@biochem.kiev.ua

The article is devoted to the analysis of the scientific and practical activity of the laboratory of the signaling mechanisms of the cells of the Palladin Institute of Biochemistry, NAS of Ukraine, in the context of the history of its development. The most important results of studies of the mechanisms controlling proliferation, migration and invasion of tumor cells, which testify to the important role of the Ruk/CIN85 adapter protein in carcinogenesis, are presented. These studies are a priority and can serve as an experimental basis for the development of new generation pharmacological agents, the targets for which can be key centers for the organization of signaling systems of the cell – adapter and scaffold proteins.

Multiple molecular forms of adaptor protein Ruk/CIN85 specifically associate with different subcellular compartments in human breast adenocarcinoma MCF-7 cells

B. O. Vynnytska-Myronovska1, Ya. P. Bobak1, G. V. Pasichnyk2,
N. I. Igumentseva1, A. A. Samoylenko2, L. B. Drobot2

1Institute of Cell Biology, National Academy of Sciences of Ukraine, Lviv;
2Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: drobot@biochem.kiev.ua

Ruk/CIN85 is a receptor-proximal ‘signalling’ adaptor that possesses three SH3 domains, Pro- and Ser-rich regions and C-terminal coiled-coil domain. It employs distinct domains and motifs to act as a transducer platform in intracellular signalling. Based on cDNA analysis, various isoforms of Ruk/CIN85 with different combination of protein-protein interaction domains as well as additional Ruk/CIN85 forms that are the products of post-translational modifications have been demonstrated. Nevertheless, there is no precise information regarding both the subcellular distribution and the role of Ruk/CIN85 multiple molecular forms in cellular responses. Using MCF-7 human breast adenocarcinoma cells and cell fractionation technique, specific association of Ruk/CIN85 molecular forms with different subcellular compartments was demonstrated. Induction of apoptosis of MCF-7 cells by doxorubicin treatment or by serum deprivation resulted in the system changes of Ruk/CIN85 molecular forms intracellular localization as well as their ratio. The data obtained provide a new insight into potential physiological significance of Ruk/CIN85 molecular forms in the regulation of various cellular functions.