Crystal structure of a PP2A B56-BubR1 complex and its implications for PP2A substrate recruitment and localization

Crystal structure of a PP2A B56-BubR1 complex and its implications for PP2A substrate recruitment and localization

ABSTRACT Protein phosphatase 2A (PP2A) accounts for the majority of total Ser/Thr phosphatase activities in most cell types and regulates many biological processes. PP2A holoenzymes contain a scaffold A subunit, a catalytic C subunit, and one of the regulatory/targeting B subunits. How the B subunit...

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Bibliographic Details
Main Authors: Jiao Wang, Zhizhi Wang, Tingting Yu, Huan Yang, David M. Virshup, Geert J. P. L. Kops, Sang Hyun Lee, Weihong Zhou, Xin Li, Wenqing Xu, Zihe Rao
Format: Article
Language:English
Published: Oxford University Press 2016-06-01
Series:Protein & Cell
Subjects:
PP2A
BubR1
kinetochore
cellular targeting
substrate recruitment
Online Access:http://link.springer.com/article/10.1007/s13238-016-0283-4

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http://link.springer.com/article/10.1007/s13238-016-0283-4

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