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PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

Abstract:

Entry into mitosis is triggered by activation of Cdk1 and inactivation of its counteracting phosphatase PP2A/B55. Greatwall kinase inactivates PP2A/B55 via its substrates Ensa and ARPP19. Both Greatwall and Ensa/ARPP19 are regulated by phosphorylation, but the dynamic regulation of Greatwall activity and the phosphatases that control Greatwall kinase and its substrates are poorly understood. To address these questions we applied a combination of mathematical modelling and experiments using ph...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1371/journal.pgen.1004004

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More from this funder
Funding agency for:
Vinod, P
Novák, B
Grant:
FP7 grant EC FP7 MitoSys (241548
FP7 grant EC FP7 MitoSys (241548
Publisher:
Public Library of Science
Journal:
PLoS Genetics More from this journal
Volume:
10
Issue:
1
Pages:
e1004004
Publication date:
2014-01-02
DOI:
EISSN:
1553-7404
ISSN:
1553-7390
Language:
English
Keywords:
Pubs id:
pubs:445855
UUID:
uuid:88de1395-c95c-4459-94d7-69a24cc03213
Local pid:
pubs:445855
Source identifiers:
445855
Deposit date:
2016-02-15

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