Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme

@article{Cho2007CrystalSO,
  title={Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme},
  author={Uhn Soo Cho and Wenqing Xu},
  journal={Nature},
  year={2007},
  volume={445},
  pages={53-57}
}
Protein phosphatase 2A (PP2A) is a principal Ser/Thr phosphatase, the deregulation of which is associated with multiple human cancers, Alzheimer’s disease and increased susceptibility to pathogen infections. How PP2A is structurally organized and functionally regulated remains unclear. Here we report the crystal structure of an AB′C heterotrimeric PP2A holoenzyme. The structure reveals that the HEAT repeats of the scaffold A subunit form a horseshoe-shaped fold, holding the catalytic C and… 
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TLDR
The first structure of a free non‐complexed B subunit, B56γ is presented, which induces the formation of a binding site for the invariant C‐terminus of the catalytic subunit that locks in the complex as a last step of assembly.
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Assembly and structure of protein phosphatase 2A
  • Yigong Shi
  • Biology
    Science in China Series C: Life Sciences
  • 2009
TLDR
Recent biochemical and structural investigation reveals critical insights into the assembly and function of the PP2A core enzyme as well as two families of holoenzyme, and a review focuses on the molecular mechanisms revealed by these latest advances.
Selection of Protein Phosphatase 2A Regulatory Subunits Is Mediated by the C Terminus of the Catalytic Subunit*
TLDR
This study shows that PP2A C subunit methylation was not absolutely required for binding the PR61/B′ and PR72/B″ subunit families, whereas binding of the PR55/B subunit family was determined by methylation and the nature of the C-terminal amino acid side chain.
Visualization of Subunit Interactions and Ternary Complexes of Protein Phosphatase 2A in Mammalian Cells
TLDR
These studies not only provide direct imaging data to support previous biochemical observations on PP2A complexes, but also offer a promising approach for studying the spatiotemporal distribution of individual PP 2A complexes in cells.
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