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Kyung S. Lee, Ph.D.
|A model illustrating the self-regulatory mechanism of PBIP1-dependent Plk1 localization and the role of Plk1 in spindle assembly checkpoint. Early in the cell cycle, PBIP1 accumulates at the interphase centromeres prior to Plk1 expression. PBIP1 is also phosphorylated to multiple tiers even before the appearance of Plk1. As Plk1 becomes abundant in G2, Plk1 interacts with PBIP1 and phosphorylates T78 to create a self-docking site for the PBD. This step is critical to promote its own recruitment to the kinetochores. In early mitosis, Plk1 degrades PBIP1 in a manner that is not understood at present. As the level of PBIP1 diminishes, Plk1 is liberated from the PBIP1 tether, and the resulting, free, Plk1 population phosphorylates 3F3/2 and other substrates critical for proper Mad2 recruitment.|
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