Fig. 5: Monomer-dimer regulation of PLK1 activity [77].
From: Structural regulation of PLK1 activity: implications for cell cycle function and drug discovery
PLK1 assumes an inactive closed and autoinhibited structure in G1 and S phases of the cell cycle. To fully sequester in an inactive state, Bora binding stabilizes dimeric PLK1 which is maintained until late G2 when Bora degradation and Aur-A phosphorylation results in a monomeric and open conformation of PLK1 which is fully activated both in terms of its catalytic activity and ability to bind to and recruit substrates in specific subcellular locations. Monomeric PLK1 has an exposed nuclear localization signal which then facilities its translocation into the nucleus. Figure was created using Biorender.
