ArticleMolecular systems biology2015
Pom1 gradient buffering through intermolecular auto-phosphorylation.
Article in Molecular systems biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Processes Controlling the Contractile Ring during Cytokinesis in Fission Yeast, Including the Role of ESCRT Proteins.Journal of fungi (Basel, Switzerland) · 2024Review
- Direct and indirect regulation of Pom1 cell size pathway by the protein phosphatase 2C Ptc1.Molecular biology of the cell · 2021Article
- Molecular Mechanism of Cytokinesis.Annual review of biochemistry · 2019Review
- Stable Pom1 clusters form a glucose-modulated concentration gradient that regulates mitotic entry.eLife · 2019Article
- Multi-phosphorylation reaction and clustering tune Pom1 gradient mid-cell levels according to cell size.eLife · 2019Article
- Mechanistic description of spatial processes using integrative modelling of noise-corrupted imaging data.Journal of the Royal Society, Interface · 2018Article
- Nine unanswered questions about cytokinesis.The Journal of cell biology · 2017Review
- Controlling cell size through sizer mechanisms.Current opinion in systems biology · 2017Review
- The role of anillin/Mid1p during medial division and cytokinesis: from fission yeast to cancer cells.Cell cycle (Georgetown, Tex.)Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 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.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.