ArticleCurrent biology : CB2016
Remodeling of the Fission Yeast Cdc42 Cell-Polarity Module via the Sty1 p38 Stress-Activated Protein Kinase Pathway.
Article in Current biology : CB, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 57 citations in OpenAlex.
- Differential gene expression drives cell-cycle-dependent transition from monopolar to bipolar growth in Schizosaccharomyces pombe.G3 (Bethesda, Md.) · 2026Article
- Temperature-specific regulation of the NDR kinase Orb6 by the MAPK Sty1 to promote heat stress resilience.Journal of cell science · 2026Article
- Constitutively active RAS prolongs Cdc42 signalling, while MAPK signalling is attenuated during fission yeast mating.PLoS genetics · 2026Article
- Control of stress-activated Cdc42 dynamics by the MAP kinase Sty1-NDR kinase Orb6 regulatory axis.iScience · 2025Article
- Rho1 and Rgf1 establish a new actin-dependent signal to determine growth poles in yeast independently of microtubules and the Tea1-Tea4 complex.PLoS biology · 2024Article
- Arp2/3-dependent endocytosis ensures Cdc42 oscillations by removing Pak1-mediated negative feedback.The Journal of cell biology · 2024Article
- The Arp2/3 complex promotes periodic removal of Pak1-mediated negative feedback to facilitate anticorrelated Cdc42 oscillations.bioRxiv : the preprint server for biology · 2023Article
- Pleiotropy drives evolutionary repair of the responsiveness of polarized cell growth to environmental cues.Frontiers in microbiology · 2023Article
- Physical properties of the cytoplasm modulate the rates of microtubule polymerization and depolymerization.Developmental cell · 2022Article
- The role of cell division control protein 42 in tumor and non-tumor diseases: A systematic review.Journal of Cancer · 2022Review
- Cdc42 reactivation at growth sites is regulated by local cell-cycle-dependent loss of its GTPase-activating protein Rga4 in fission yeast.Journal of cell science · 2021Article
- Cell patterning by secretion-induced plasma membrane flows.Science advances · 2021Article
- Variations of intracellular density during the cell cycle arise from tip-growth regulation in fission yeast.eLife · 2021Article
- Review
- Stress-Activated Protein Kinase Signalling Regulates Mycoparasitic Hyphal-Hyphal Interactions inJournal of fungi (Basel, Switzerland) · 2021Article
- Genes affecting the extension of chronological lifespan in Schizosaccharomyces pombe (fission yeast).Molecular microbiology · 2021Review
- Microtubule-independent movement of the fission yeast nucleus.Journal of cell science · 2021Article
- Article
- Article
- Optogenetics reveals Cdc42 local activation by scaffold-mediated positive feedback and Ras GTPase.PLoS biology · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Rho family GTPase Cdc42 is a key regulator of eukaryotic cellular organization and cell polarity [1]. In the fission yeast Schizosaccharomyces pombe, active Cdc42 and associated effectors and regulators (the "Cdc42 polarity module") coordinate polarized growth at cell tips by controlling the actin cytoskeleton and exocytosis [2-4]. Localization of the Cdc42 polarity module to cell tips is thus critical for its function. Here we show that the fission yeast stress-activated protein kinase Sty1, a homolog of mammalian p38 MAP kinase, regulates localization of the Cdc42 polarity module. In wild-type cells, treatment with latrunculin A, a drug that leads to actin depolymerization, induces dispersal of the Cdc42 module from cell tips and cessation of polarized growth [5, 6]. We show that latrunculin A treatment also activates the Sty1 MAP kinase pathway and, strikingly, we find that loss of Sty1 MAP kinase signaling prevents latrunculin A-induced dispersal of the Cdc42 module, allowing polarized growth even in complete absence of the actin cytoskeleton. Regulation of the Cdc42 module by Sty1 is independent of Sty1's role in stress-induced gene expression. We also describe a system for activation of Sty1 kinase "on demand" in the absence of any external stress, and use this to show that Sty1 activation alone is sufficient to disperse the Cdc42 module from cell tips in otherwise unperturbed cells. During nitrogen-starvation-induced quiescence, inhibition of Sty1 converts non-growing, depolarized cells into growing, polarized cells. Our results place MAP kinase Sty1 as an important physiological regulator of the Cdc42 polarity module.
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