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

Détails

Cette publication a été rétractée.
Ressource 1Télécharger: BIB_F2038D08BF68.P001.pdf (10667.02 [Ko])
Etat: Public
Version: Final published version
ID Serval
serval:BIB_F2038D08BF68
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Retraction Notice of the Article: The DYRK-family kinase Pom1 phosphorylates the F-BAR protein Cdc15 to prevent division at cell poles
Périodique
The Journal of cell biology
Auteur(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
Statut éditorial
Publié
Date de publication
2017
Peer-reviewed
Oui
Volume
211
Numéro
3
Pages
653-668
Langue
anglais
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

Résumé
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.

Mots-clé
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
Oui
Création de la notice
27/02/2017 13:51
Dernière modification de la notice
20/08/2019 16:19
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