Pom1 gradient buffering through intermolecular auto-phosphorylation.

Détails

Ressource 1Télécharger: BIB_8A9B72AA03B4.P001.pdf (984.52 [Ko])
Etat: Serval
Version: Final published version
ID Serval
serval:BIB_8A9B72AA03B4
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Pom1 gradient buffering through intermolecular auto-phosphorylation.
Périodique
Molecular Systems Biology
Auteur(s)
Hersch M., Hachet O., Dalessi S., Ullal P., Bhatia P., Bergmann S., Martin S.G.
ISSN
1744-4292 (Electronic)
ISSN-L
1744-4292
Statut éditorial
Publié
Date de publication
2015
Peer-reviewed
Oui
Volume
11
Numéro
7
Pages
818
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Résumé
Concentration gradients provide spatial information for tissue patterning and cell organization, and their robustness under natural fluctuations is an evolutionary advantage. In rod-shaped Schizosaccharomyces pombe cells, the DYRK-family kinase Pom1 gradients control cell division timing and placement. Upon dephosphorylation by a Tea4-phosphatase complex, Pom1 associates with the plasma membrane at cell poles, where it diffuses and detaches upon auto-phosphorylation. Here, we demonstrate that Pom1 auto-phosphorylates intermolecularly, both in vitro and in vivo, which confers robustness to the gradient. Quantitative imaging reveals this robustness through two system's properties: The Pom1 gradient amplitude is inversely correlated with its decay length and is buffered against fluctuations in Tea4 levels. A theoretical model of Pom1 gradient formation through intermolecular auto-phosphorylation predicts both properties qualitatively and quantitatively. This provides a telling example where gradient robustness through super-linear decay, a principle hypothesized a decade ago, is achieved through autocatalysis. Concentration-dependent autocatalysis may be a widely used simple feedback to buffer biological activities.
Mots-clé
Algorithms, Cell Division, Cell Membrane/metabolism, Microtubule-Associated Proteins/metabolism, Phosphorylation, Protein Kinases/chemistry, Protein Kinases/metabolism, Schizosaccharomyces/enzymology, Schizosaccharomyces pombe Proteins/metabolism
Pubmed
Web of science
Création de la notice
27/08/2015 10:50
Dernière modification de la notice
03/03/2018 19:10
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