Phospho-regulation of nuclear localization modules by Cdk1

Abstract

The cells are subjects to many internal events such as the cell cycle which results in cell proliferation. The cell cycle events are regulated by protein phosphorylation done by cyclindependent kinases (CDKs) which target specific targets in well-timed manner using binding partners known as cyclins and cyclin-dependent protein kinase regulatory subunits. The changes induced by such complexes can affect protein subcellular localization by activating or inhibiting nuclear localization sequences (NLS) and nuclear export signals (NES) - amino acid regions, recognized by dedicated shuttling proteins. In this thesis the influence of cyclin specificity on protein nuclear localization patterns in Cdk1 targets, containing cyclin docking regions, is studied. Specific experiments are conducted on Dna2(1-100) and Psy4(315-441) which are two truncated modules of original proteins known for subcellular localization dependence on the cell cycle.