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Pom1 gradient buffering through intermolecular auto-phosphorylation

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Publication date 2015
Author Hersch Micha, Hachet Olivier, Dalessi Sascha, Ullal Pranav, Bhatia Payal, Bergmann Sven, Martin Sophie,
Project Cell polarization in response to intra- and extracellular cues in fission yeast
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Original article (peer-reviewed)

Journal Molecular systems biology
Volume (Issue) 11
Page(s) 818
Title of proceedings Molecular systems biology
DOI DOI 10.15252/msb.20145996

Open Access

URL http://msb.embopress.org/content/11/7/818
Type of Open Access Website

Abstract

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 autophosphorylation 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.
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