ArticleThe EMBO journal1998
Fusion pore expansion in horse eosinophils is modulated by Ca2+ and protein kinase C via distinct mechanisms.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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Who cites it
35 citing papers in PubMed, 117 citations in OpenAlex.
- Fusion Pores as Regulators of Quantal Size and Cellular Physiology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- The neuronal calcium sensor Synaptotagmin-1 and SNARE proteins cooperate to dilate fusion pores.eLife · 2021Article
- Mitochondrial hydrogen peroxide positively regulates neuropeptide secretion during diet-induced activation of the oxidative stress response.Nature communications · 2021Article
- Article
- Differential Release of Exocytosis Marker Dyes Indicates Stimulation-Dependent Regulation of Synaptic Activity.Frontiers in neuroscience · 2019Article
- Article
- Application of High-Throughput Assays to Examine Phospho-Modulation of the Late Steps of Regulated Exocytosis.High-throughput · 2017Article
- Fusion pores and their control of neurotransmitter and hormone release.The Journal of general physiology · 2017Review
- Striatal dopamine neurotransmission: regulation of release and uptake.Basal ganglia · 2016Article
- Synaptotagmin-7 links fusion-activated Ca²⁺ entry and fusion pore dilation.Journal of cell science · 2014Article
- The role of Pak-interacting exchange factor-β phosphorylation at serines 340 and 583 by PKCγ in dopamine release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- High resolution electrophysiological techniques for the study of calcium-activated exocytosis.Biochimica et biophysica acta · 2012Review
- Vesicular calcium channels as regulators of the exocytotic post-fusion phase.Communicative & integrative biology · 2011Article
- Fusion-activated Ca2+ entry via vesicular P2X4 receptors promotes fusion pore opening and exocytotic content release in pneumocytes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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- New insights into the control of secretion.Communicative & integrative biology · 2009Article
- F-actin and myosin II accelerate catecholamine release from chromaffin granules.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- The role of the C terminus of the SNARE protein SNAP-25 in fusion pore opening and a model for fusion pore mechanics.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- PKC theta activity maintains normal quantal size in chromaffin cells.Journal of neurochemistry · 2008Article
- Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin.The Journal of general physiology · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using the patch-clamp technique, we studied the role of protein phosphorylation and dephosphorylation on the exocytotic fusion of secretory granules with the plasma membrane in horse eosinophils. Phorbol 12-myristate 13-acetate (PMA) had no effect on the amplitude and dynamics of degranulation, indicating that the formation of fusion pores is insensitive to activation of protein kinase C (PKC). Fusion pore expansion, however, was accelerated approximately 2-fold by PMA, and this effect was abolished by staurosporine. Elevating intracellular Ca2+ to 1.5 microM also resulted in a 2-fold acceleration of pore expansion; this effect was not prevented by staurosporine, indicating that intracellular Ca2+ and activation of PKC accelerate fusion pore expansion via distinct mechanisms. However, fusion pores can expand fully even when PKC is inhibited. In contrast, the phosphatase inhibitor alpha-naphthylphosphate inhibits exocytotic fusion and slows fusion pore expansion. These results demonstrate that, subsequent to its formation, fusion pore expansion is under control of proteins subject to functional changes based on their phosphorylation states.
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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.