PP2A Cdc55 Phosphatase Imposes Ordered Cell-Cycle Phosphorylation by Opposing Threonine Phosphorylation-Reference-Cited by-同舟云学术

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PP2A Cdc55 Phosphatase Imposes Ordered Cell-Cycle Phosphorylation by Opposing Threonine Phosphorylation

Published:2017-02 Issue:3 Volume:65 Page:393-402.e3
ISSN:1097-2765
Container-title:Molecular Cell
language:en
Short-container-title:Molecular Cell

Author:

Godfrey Molly,Touati Sandra A.,Kataria Meghna,Jones Andrew,Snijders Ambrosius P.,Uhlmann Frank

Funder

Cancer Research UK

UK Medical Research Council

Wellcome Trust

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference53 articles.

1. Synthetic peptides as model substrates for the study of the specificity of the polycation-stimulated protein phosphatases;Agostinis;Eur. J. Biochem.,1990

2. Specificity of the polycation-stimulated (type-2A) and ATP,Mg-dependent (type-1) protein phosphatases toward substrates phosphorylated by P34cdc2 kinase;Agostinis;Eur. J. Biochem.,1992

3. Cyclin-specific docking motifs promote phosphorylation of yeast signaling proteins by G1/S Cdk complexes;Bhaduri;Curr. Biol.,2011

4. A quantitative model for ordered Cdk substrate dephosphorylation during mitotic exit;Bouchoux;Cell,2011

5. Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine;Bremmer;J. Biol. Chem.,2012

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