A PP2A-B55 recognition signal controls substrate dephosphorylation kinetics during mitotic exit
Author:
Affiliation:
1. Department of Biochemistry, University of Oxford, Oxford OX1 3QU, England, UK
2. Department of Chemistry, University of Oxford, Oxford OX1 3TA, England, UK
Abstract
Funder
Cancer Research UK
Boehringer Ingelheim Fonds
Engineering and Physical Sciences Research Council
Wellcome Trust
Biotechnology and Biological Sciences Research Council
Publisher
Rockefeller University Press
Subject
Cell Biology
Link
http://rupress.org/jcb/article-pdf/214/5/539/1373205/jcb_201606033.pdf
Reference44 articles.
1. Spatial exclusivity combined with positive and negative selection of phosphorylation motifs is the basis for context-dependent mitotic signaling;Alexander;Sci. Signal.,2011
2. KIF4A and PP2A-B56 form a spatially restricted feedback loop opposing Aurora B at the anaphase central spindle;Bastos;J. Cell Biol.,2014
3. Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics;Boersema;Nat. Protoc.,2009
4. A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit;Bouchoux;Cell.,2011
5. The M phase kinase Greatwall (Gwl) promotes inactivation of PP2A/B55delta, a phosphatase directed against CDK phosphosites;Castilho;Mol. Biol. Cell.,2009
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