PLK1

PLK1 protein kinase (also polo-like kinase 1 ) is an enzyme in eukaryotes, known as a kinase which phosphorylates a variety of proteins in the nucleus and thus exert a regulatory function during cell division. Enabled is PLK1 by growth-promoting factors. Human PLK1 is particularly localized in the nuclei of placental and gut tissue, and is produced excessively in some tumors. Therefore, inhibitors of the enzyme are considered as potential drugs against cancer.

PLK1 is one of the polo-like kinases. There are mitotic kinases. ie, those which are involved in the regulation of the cell cycle. There are serine / threonine kinases that are present are highly conserved in different species.

Structure

PLK1 is composed of 603 amino acids at the amino terminus of a catalytic domain (which can be divided into eleven subdomains ) and three conserved polo boxes at the carboxy terminus. You control the function of PLK1 during mitosis and cellular localization.

Function

PLK1 has a variety of functions in the cell, to the main part of the phosphorylation and thus activation of the cyclin-dependent phosphatase, Cdc25, which is required for formation of the bipolar spindle during prometaphase the cell cycle. In addition, Plk 1 interacts with APC, the anaphase -promoting -complex, which is responsible for the degradation of mitotic proteins.

PLK1 is highly expressed in proliferating tissue and appears to be over-expressed in a number of tumor tissues. Inhibitors of PLK1, such as BI 7278, therefore, are important candidates for new therapeutic approaches in cancer therapy.

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