Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25
Open accessAbstract
Protein kinase A (PKA) is a key regulator of neurosecretion, but the molecular targets remain elusive. We combined pharmacological manipulations of kinase and phosphatase activities with mutational studies on the exocytotic machinery driving fusion of catecholamine-containing vesicles from chromaffin cells. We found that constitutive PKA activity was necessary to maintain a large number of vesicles in the release-ready, so-called primed, state, whereas calcineurin (protein phosphatase 2B) activity antagonized this effect. Overexpression of the SNARE protein SNAP-25a mutated in a PKA phosphorylation site (Thr-138) eliminated the effect of PKA inhibitors on the vesicle priming process. Another, unidentified, PKA target regulated the relative size of two different primed vesicle pools that are distinguished by their release kinetics. Overexpression of the SNAP-25b isoform increased the size of both primed vesicle pools by a factor of two, and mutations in the conserved Thr-138 site had similar effects as in the a isoform.
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Phosphorylation of SNAP 25 protein by PKA affected the size of the releasable pool in chromaffin cells.
“For example, phosphorylation of SNAP 25 protein by PKA affected the size of the releasable pool in chromaffin cells [93].”
From Presynaptic cAMP-PKA-mediated potentiation induces reconfiguration of synaptic vesicle pools and channel-vesicle coupling at hippocampal mossy fiber boutons (2024) · cites this paper as [93]
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References 65 · Cited by 239
- Authors
- Nagy, G., Reim, K., Matti, U., Brose, N., Binz, T., Rettig, J., Neher, E., & Sørensen, J. B.
- Affiliations
- Max Planck Institute for Biophysical Chemistry (DE)
- Max Planck Institute of Experimental Medicine (DE)
- Medizinische Hochschule Hannover (DE)
- Corresponding author
- Sørensen, Jakob B
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 41
- Issue
- 3
- Pages
- 417-429
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W1998983314
- Cited by
- 239
- References
- 65
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 13 · 2023: 11 · 2022: 5 · 2021: 6 · 2020: 3 · 2019: 5 · 2018: 7 · 2017: 9 · 2016: 7 · 2015: 4 · 2014: 11 · 2013: 10 · 2012: 15
- FWCI
- 9.93
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3454 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- GRO (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, cc-by)
- Funders
- Universität des Saarlandes
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- protein kinase A, SNAP-25, vesicle priming, exocytosis, chromaffin cells, catecholamine release, calcineurin, SNARE proteins, release kinetics
- MeSH terms
- Cyclic AMP, Alanine, Animals, Calcium, Carbazoles, Carrier Proteins, Catecholamines, Cattle, Cells, Cultured, Drug Interactions, Embryo, Mammalian, Enzyme Inhibitors, Exocytosis, Colforsin, Humans, Indoles, Kidney, Membrane Potentials, Membrane Proteins, Models, Biological, Mutation, Nerve Tissue Proteins, Peptide Fragments, Phosphorylation, Photolysis, Pyrethrins, Pyrroles, Threonine, Time Factors, Transfection, Blotting, Western, Cyclic AMP-Dependent Protein Kinases, Patch-Clamp Techniques, Chromaffin Cells, Calcineurin, Secretory Vesicles, Intracellular Signaling Peptides and Proteins, Synaptosomal-Associated Protein 25
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