西亚试剂：Structure of a Protein Phosphatase 2A Holoenzyme: Insights

Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation

Yanhui Xu,¹,²,³ Yu Chen,¹,² Ping Zhang,¹ Philip D. Jeffrey,¹ and Yigong Shi¹,⁴,

¹ Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, Princeton, NJ 08544, USA

2 These authors contributed equally to this work
3 Present address: Institute of Biomedical Sciences, Fudan University, Shanghai 200032, China
4 Present address: Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China

Protein phosphatase 2A (PP2A) regulates many essential aspects of cellular physiology. Members of the regulatory B/B55/PR55 family are thought to play a key role in the dephosphorylation of Tau, whose hyperphosphorylation contributes to Alzheimer's disease. The underlying mechanisms of the PP2A-Tau connection remain largely enigmatic. Here, we report the complete reconstitution of a Tau dephosphorylation assay and the crystal structure of a heterotrimeric PP2A holoenzyme involving the regulatory subunit Bα. We show that Bα specifically and markedly facilitates dephosphorylation of the phosphorylated Tau in our reconstituted assay. The Bα subunit comprises a seven-bladed β propeller, with an acidic, substrate-binding groove located in the center of the propeller. The β propeller latches onto the ridge of the PP2A scaffold subunit with the help of a protruding β hairpin arm. Structure-guided mutagenesis studies revealed the underpinnings of PP2A-mediated dephosphorylation of Tau.

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