Retraction Notice of the Article: The DYRK-family kinase Pom1 phosphorylates the F-BAR protein Cdc15 to prevent division at cell poles

Details

This publication has been retracted.
Ressource 1Download: BIB_F2038D08BF68.P001.pdf (10667.02 [Ko])
State: Public
Version: Final published version
Serval ID
serval:BIB_F2038D08BF68
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Retraction Notice of the Article: The DYRK-family kinase Pom1 phosphorylates the F-BAR protein Cdc15 to prevent division at cell poles
Journal
The Journal of cell biology
Author(s)
Ullal P., McDonald N.A., Chen J.S., Lo Presti L., Roberts-Galbraith R.H., Gould K.L., Martin S.G.
ISSN
1540-8140 (Electronic)
ISSN-L
0021-9525
Publication state
Published
Issued date
2017
Peer-reviewed
Oui
Volume
211
Number
3
Pages
653-668
Language
english
Notes
Retraction i of
The DYRK-family kinase Pom1 phosphorylates the F-BAR protein Cdc15 to prevent division at cell poles. [J Cell Biol. 2015]
PMID: 28209645 DOI: 10.1083/jcb.20150407302062017r

Abstract
Division site positioning is critical for both symmetric and asymmetric cell divisions. In many organisms, positive and negative signals cooperate to position the contractile actin ring for cytokinesis. In rod-shaped fission yeast Schizosaccharomyces pombe cells, division at midcell is achieved through positive Mid1/anillin-dependent signaling emanating from the central nucleus and negative signals from the dual-specificity tyrosine phosphorylation-regulated kinase family kinase Pom1 at the cell poles. In this study, we show that Pom1 directly phosphorylates the F-BAR protein Cdc15, a central component of the cytokinetic ring. Pom1-dependent phosphorylation blocks Cdc15 binding to paxillin Pxl1 and C2 domain protein Fic1 and enhances Cdc15 dynamics. This promotes ring sliding from cell poles, which prevents septum assembly at the ends of cells with a displaced nucleus or lacking Mid1. Pom1 also slows down ring constriction. These results indicate that a strong negative signal from the Pom1 kinase at cell poles converts Cdc15 to its closed state, destabilizes the actomyosin ring, and thus promotes medial septation.

Keywords
Actomyosin/metabolism, Cell Cycle Proteins/metabolism, Cell Division/physiology, Cytokinesis/physiology, Cytoskeletal Proteins/metabolism, GTP-Binding Proteins/metabolism, Phosphorylation/physiology, Protein Kinases/metabolism, Protein-Serine-Threonine Kinases/metabolism, Protein-Tyrosine Kinases/metabolism, Schizosaccharomyces/metabolism, Schizosaccharomyces pombe Proteins/metabolism
Pubmed
Web of science
Open Access
Yes
Create date
27/02/2017 13:51
Last modification date
20/08/2019 16:19
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