标题
PP2A/B55 and Fcp1 Regulate Greatwall and Ensa Dephosphorylation during Mitotic Exit
作者
关键词
-
出版物
PLoS Genetics
Volume 10, Issue 1, Pages e1004004
出版商
Public Library of Science (PLoS)
发表日期
2014-01-03
DOI
10.1371/journal.pgen.1004004
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Bypassing the Greatwall-Endosulfine Pathway: Plasticity of a Pivotal Cell-Cycle Regulatory Module in Drosophila melanogaster and Caenorhabditis elegans
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- Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit
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- MASTL is the human ortholog of Greatwall kinase that facilitates mitotic entry, anaphase and cytokinesis
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- Vertebrate cells genetically deficient for Cdc14A or Cdc14B retain DNA damage checkpoint proficiency but are impaired in DNA repair
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- Loss of human Greatwall results in G2 arrest and multiple mitotic defects due to deregulation of the cyclin B-Cdc2/PP2A balance
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- The Substrate of Greatwall Kinase, Arpp19, Controls Mitosis by Inhibiting Protein Phosphatase 2A
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- Greatwall maintains mitosis through regulation of PP2A
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- Regulated activity of PP2A–B55δ is crucial for controlling entry into and exit from mitosis in Xenopus egg extracts
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- Analysis of All Protein Phosphatase Genes inAspergillus nidulansIdentifies a New Mitotic Regulator, Fcp1
- (2009) Sunghun Son et al. EUKARYOTIC CELL
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- (2009) Arne Lindqvist et al. JOURNAL OF CELL BIOLOGY
- The M Phase Kinase Greatwall (Gwl) Promotes Inactivation of PP2A/B55δ, a Phosphatase Directed Against CDK Phosphosites
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