ArticleEuropean journal of cell biology2012
Perturbations of the actin cytoskeleton activate a Dictyostelium STAT signalling pathway.
Article in European journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Profilin-1 Deficiency Activates STING to Drive T Cell-Mediated Anti-Tumor Immunity in Breast Cancer.bioRxiv : the preprint server for biology · 2026Article
- Osmosensing and osmoregulation in unicellular eukaryotes.World journal of microbiology & biotechnology · 2015Review
- The Dictyostelium prestalk inducer differentiation-inducing factor-1 (DIF-1) triggers unexpectedly complex global phosphorylation changes.Molecular biology of the cell · 2015Article
- Two Dictyostelium tyrosine kinase-like kinases function in parallel, stress-induced STAT activation pathways.Molecular biology of the cell · 2014Article
- The arrestin-domain containing protein AdcA is a response element to stress.Cell communication and signaling : CCS · 2013Article
- Identification of the kinase that activates a nonmetazoan STAT gives insights into the evolution of phosphotyrosine-SH2 domain signaling.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Dictyostelium transcription factor STATc is tyrosine phosphorylated and accumulates in the nucleus when cells are exposed either to hyper-osmotic stress or to the prestalk-inducing polyketide DIF-1. In the case of stress STAT activation is mediated by regulated dephosphorylation; whereby two serine residues on PTP3, the tyrosine phosphatase that de-activates STATc, become phosphorylated after exposure to stress so inhibiting enzymatic activity. We now show that the more highly regulated of the two PTP3 serine residues, S747, is also phosphorylated in response to DIF-1, suggesting a common activation mechanism. Hyper-osmotic stress causes a re-distribution of F-actin to the cortex, cell rounding and shrinkage and we show that DIF-1 induces a similar but transient F-actin re-distribution and rounding response. We also find that two mechanistically distinct inhibitors of actin polymerization, latrunculin A and cytochalasin A induce phosphorylation at S747 of PTP3 and activate STATc. We suggest that PTP3 phosphorylation, and consequent STATc activation, are regulated by changes in F-actin polymerization status during stress and DIF-induced cytoskeletal remodelling.
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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.