Centromeric binding and activity of Protein Phosphatase 4
Centromeric binding and activity of Protein Phosphatase 4
The cell division cycle requires tight coupling between protein phosphorylation and dephosphorylation. However, understanding the cell cycle roles of multimeric protein phosphatases has been limited by the lack of knowledge of how their diverse regulatory subunits target highly conserved catalytic subunits to their sites of action. Phosphoprotein phosphatase 4 (PP4) has been recently shown to participate in the regulation of cell cycle progression. We now find that the EVH1 domain of the regulatory subunit 3 of Drosophila PP4, Falafel (Flfl), directly interacts with the centromeric protein C (CENP-C). Unlike other EVH1 domains that interact with proline-rich ligands, the crystal structure of the Flfl amino-terminal EVH1 domain bound to a CENP-C peptide reveals a new target-recognition mode for the phosphatase subunit. We also show that binding of Flfl to CENP-C is required to bring PP4 activity to centromeres to maintain CENP-C and attached core kinetochore proteins at chromosomes during mitosis.
1-13
Lipinszki, Zoltan
e405fd6d-1bee-4725-96b7-7c315f2826ed
Lefevre, Stephane
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Savoian, Matthew S.
030193ef-9e94-48bb-ab02-f5700d1622a7
Singleton, Martin R.
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Glover, David M.
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Przewloka, Marcin
9b25e73c-ec15-43df-a5a4-ac9574bb20ab
6 January 2015
Lipinszki, Zoltan
e405fd6d-1bee-4725-96b7-7c315f2826ed
Lefevre, Stephane
ba49d47d-03fb-4e92-addc-f657e555617e
Savoian, Matthew S.
030193ef-9e94-48bb-ab02-f5700d1622a7
Singleton, Martin R.
4cec84f3-a217-434c-992c-ff983ee2fc59
Glover, David M.
cca9cd19-3e1e-4906-b418-41876c1f9c61
Przewloka, Marcin
9b25e73c-ec15-43df-a5a4-ac9574bb20ab
Lipinszki, Zoltan, Lefevre, Stephane, Savoian, Matthew S., Singleton, Martin R., Glover, David M. and Przewloka, Marcin
(2015)
Centromeric binding and activity of Protein Phosphatase 4.
Nature Communications, 6, , [5894].
(doi:10.1038/ncomms6894).
(PMID:25562660)
Abstract
The cell division cycle requires tight coupling between protein phosphorylation and dephosphorylation. However, understanding the cell cycle roles of multimeric protein phosphatases has been limited by the lack of knowledge of how their diverse regulatory subunits target highly conserved catalytic subunits to their sites of action. Phosphoprotein phosphatase 4 (PP4) has been recently shown to participate in the regulation of cell cycle progression. We now find that the EVH1 domain of the regulatory subunit 3 of Drosophila PP4, Falafel (Flfl), directly interacts with the centromeric protein C (CENP-C). Unlike other EVH1 domains that interact with proline-rich ligands, the crystal structure of the Flfl amino-terminal EVH1 domain bound to a CENP-C peptide reveals a new target-recognition mode for the phosphatase subunit. We also show that binding of Flfl to CENP-C is required to bring PP4 activity to centromeres to maintain CENP-C and attached core kinetochore proteins at chromosomes during mitosis.
Text
ncomms6894.pdf
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Accepted/In Press date: 18 November 2014
Published date: 6 January 2015
Organisations:
Molecular and Cellular, Centre for Biological Sciences
Identifiers
Local EPrints ID: 393857
URI: http://eprints.soton.ac.uk/id/eprint/393857
PURE UUID: 198d8c99-219f-4934-8c7e-14cb5954a694
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Date deposited: 09 May 2016 09:17
Last modified: 15 Mar 2024 03:54
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Contributors
Author:
Zoltan Lipinszki
Author:
Stephane Lefevre
Author:
Matthew S. Savoian
Author:
Martin R. Singleton
Author:
David M. Glover
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