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A PP2A-B55 recognition signal controls substrate dephosphorylation kinetics during mitotic exit

Abstract:

PP2A-B55 is one of the major phosphatases regulating cell division. Despite its importance for temporal control during mitotic exit, how B55 substrates are recognised and differentially dephosphorylated is unclear. Using phosphoproteomics combined with kinetic modelling to extract B55-dependent rate constants, we have systematically identified B55 substrates and assigned their temporal order in mitotic exit. These substrates share a bipartite polybasic recognition determinant (BPR) flanking a...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1083/jcb.201606033

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Funding agency for:
Hutter, L
Grant:
EPG03706X/1
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Funding agency for:
Holder, J
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Funding agency for:
Novak, B
Grant:
BB/M00354X/1
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Funding agency for:
Barr, F
Grant:
C20079/A15940
Publisher:
Rockefeller University Press Publisher's website
Journal:
Journal of Cell Biology Journal website
Publication date:
2016-08-22
Acceptance date:
2016-07-13
DOI:
EISSN:
1540-8140
ISSN:
0021-9525
Source identifiers:
637868
Keywords:
Pubs id:
pubs:637868
UUID:
uuid:c211d4a1-c4bf-486d-891a-567458695ca8
Local pid:
pubs:637868
Deposit date:
2016-08-08

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