Scientific article
Open access

Pom1 gradient buffering through intermolecular auto‐phosphorylation

Published inMolecular systems biology, vol. 11, no. 7, 818
Publication date2015-07-06
First online date2015-07-06

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 dephos-phorylation 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 auto-catalysis may be a widely used simple feedback to buffer biological activities.

  • Auto‐catalysis
  • Cell cycle control
  • Fission yeast Schizosaccharomyces pombe
  • Gradient formation
  • Robustness
Affiliation Not a UNIGE publication
Citation (ISO format)
HERSCH, Micha et al. Pom1 gradient buffering through intermolecular auto‐phosphorylation. In: Molecular systems biology, 2015, vol. 11, n° 7, p. 818. doi: 10.15252/msb.20145996
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Article (Published version)
ISSN of the journal1744-4292

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