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Self-priming of Plk1 binding to BubR1 ensures accurate mitotic progression. | LitMetric

AI Article Synopsis

  • - Plk1 is a crucial kinase that ensures proper cell division by interacting with various proteins, but the binding mechanisms are more complex than previously thought, requiring more research to understand them.
  • - During mitosis, Plk1 interacts with the checkpoint protein BubR1 by phosphorylating specific sites, which enhances its interaction with PP2A/B56, essential for stabilizing kinetochore-microtubule attachments.
  • - The study shows that phosphorylation of BubR1 at T600/T608 by Plk1 is vital for its function; however, modifying BubR1 to increase its affinity for Plk1 and PP2A/B56 can compensate for the need for phosphorylation, highlighting new regulatory mechanisms for mit

Article Abstract

Plk1 is a key mitotic kinase that localizes to distinct subcellular structures to promote accurate mitotic progression. Plk1 recruitment depends on direct interaction between polo-box domain (PBD) on Plk1 and PBD binding motif (PBD BM) on the interactors. However, recent study showed that PBD BM alone is not enough for stable binding between CENP-U and Plk1 highlighting the complexity of the interaction which warrants further investigation. An important interactor for Plk1 during mitosis is the checkpoint protein BubR1. Plk1 bound to BubR1 via PBD interaction with pT620 phosphorylates BubR1 S676/T680 to promote BubR1-PP2A/B56 interaction. The BubR1-PP2A/B56 complex counteracts the destablizing effect on kinetochore-microtubule attachments by mitotic kinases to promote mitotic progression. Here we show that Plk1 phosphorylates T600/T608 on BubR1 and the double phosphorylation is critical for BubR1-Plk1 interaction. A similar mechanism for Plk1-Bub1 interaction also exists indicating a general principle for Plk1 kinetochore recruitment through self-priming. Mechanistically preventing BubR1 T600/T608 phosphorylation impairs chromosome congression and checkpoint silencing by reducing Plk1 and PP2A/B56 binding to BubR1. Increasing the binding affinity towards Plk1 and PP2A/B56 in BubR1 through protein engineering bypasses the requirement of T600/T608 phosphorylation for mitotic progression. These results reveal a new layer of regulation for accurate mitotic progression.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11549336PMC
http://dx.doi.org/10.1038/s42003-024-07205-2DOI Listing

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