AI Article Synopsis

  • Shugoshin proteins play a crucial role in protecting centromeric cohesin during both mitosis and meiosis.
  • The study focuses on the interaction between human hSgo1 and the PP2A-B56 phosphatase, uncovering new details about their structural formation and functional dynamics.
  • Key findings show that a specific conserved pocket on B56 is essential for hSgo1 binding, which inhibits the binding of certain substrates and allows for the dephosphorylation of Cdk1 sites on hSgo1, thereby influencing cohesin interactions.

Article Abstract

The shugoshin proteins are universal protectors of centromeric cohesin during mitosis and meiosis. The binding of human hSgo1 to the PP2A-B56 phosphatase through a coiled-coil (CC) region mediates cohesion protection during mitosis. Here we undertook a structure function analysis of the PP2A-B56-hSgo1 complex, revealing unanticipated aspects of complex formation and function. We establish that a highly conserved pocket on the B56 regulatory subunit is required for hSgo1 binding and cohesion protection during mitosis in human somatic cells. Consistent with this, we show that hSgo1 blocks the binding of PP2A-B56 substrates containing a canonical B56 binding motif. We find that PP2A-B56 bound to hSgo1 dephosphorylates Cdk1 sites on hSgo1 itself to modulate cohesin interactions. Collectively our work provides important insight into cohesion protection during mitosis.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8256288PMC
http://dx.doi.org/10.15252/embr.202052295DOI Listing

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