Centromeric binding and activity of Protein Phosphatase 4.

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Lipinszki Z,Lefevre S,Savoian MS,Singleton MR,Glover DM,Przewloka MR

doi

10.1038/ncomms6894

subject

Has Abstract

pub_date

2015-01-06 00:00:00

pages

5894

issn

2041-1723

pii

ncomms6894

journal_volume

6

pub_type

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