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The structural basis for tight control of PP2A methylation and function by LCMT-1
Authors:Stanevich Vitali  Jiang Li  Satyshur Kenneth A  Li Yongfeng  Jeffrey Philip D  Li Zhu  Menden Patrick  Semmelhack Martin F  Xing Yongna
Institution:McArdle Laboratory, Department of Oncology, School of Medicine and Public Health, University of Wisconsin at Madison, Madison, WI 53706, USA.
Abstract:
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  • Highlights? LCMT-1 makes extensive contacts to PP2A active site for methylation of PP2A tail ? PP2A methylation is stimulated by phosphatase activation, hampered by inactivation ? LCMT-1 would facilitate efficient transition of activated PP2A to holoenzymes ? A high-affinity dnLCMT-1 mutant attenuates the cell cycle without causing cell death
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