Journal article
A PP2A-B55 recognition signal controls substrate dephosphorylation kinetics during mitotic exit
- Abstract:
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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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(Version of record, pdf, 3.9MB)
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- Publisher copy:
- 10.1083/jcb.201606033
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Authors
Funding
+ Engineering and Physical Sciences Research Council
More from this funder
Funding agency for:
Hutter, L
Grant:
EPG03706X/1
+ Biotechnological and Biological Sciences Research
More from this funder
Funding agency for:
Novak, B
Grant:
BB/M00354X/1
Bibliographic Details
- 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:
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1540-8140
- ISSN:
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0021-9525
- Source identifiers:
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637868
Item Description
- Keywords:
- Pubs id:
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pubs:637868
- UUID:
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uuid:c211d4a1-c4bf-486d-891a-567458695ca8
- Local pid:
- pubs:637868
- Deposit date:
- 2016-08-08
Terms of use
- Copyright holder:
- Cundell, et al
- Copyright date:
- 2016
- Notes:
- © 2016 Cundell et al. This article is distributed under the terms of an Attribution– Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
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