ArticleThe Journal of cell biology1987
Synapsin I: an actin-bundling protein under phosphorylation control.
Article in The Journal of cell biology, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 176 citations in OpenAlex.
- Phosphoproteomic profiling reveals reversal of dysregulated kinase signaling by nitric oxide inhibition in the Shank3 mouse model of autism.Scientific reports · 2026Article
- Condensates of synaptic vesicles and synapsin-1 mediate actin sequestering and polymerization.The EMBO journal · 2025Article
- Condensates of synaptic vesicles and synapsin are molecular beacons for actin sequestering and polymerization.bioRxiv : the preprint server for biology · 2025Article
- Crosstalk of Synapsin1 palmitoylation and phosphorylation controls the dynamicity of synaptic vesicles in neurons.Cell death & disease · 2022Article
- Synapsin 1 promotes Aβ generation via BACE1 modulation.PloS one · 2019Article
- Microwave & magnetic (M2) proteomics reveals CNS-specific protein expression waves that precede clinical symptoms of experimental autoimmune encephalomyelitis.Scientific reports · 2014Article
- Is replenishment of the readily releasable pool associated with vesicular movement?Cognitive neurodynamics · 2014Article
- Polyelectrolyte properties of filamentous biopolymers and their consequences in biological fluids.Soft matter · 2014Review
- P-Rex2, a Rac-guanine nucleotide exchange factor, is expressed selectively in ribbon synaptic terminals of the mouse retina.BMC neuroscience · 2013Article
- Overexpression of synapsin Ia in the rat calyx of Held accelerates short-term plasticity and decreases synaptic vesicle volume and active zone area.Frontiers in cellular neuroscience · 2013Article
- Synaptic vesicle mobility in mouse motor nerve terminals with and without synapsin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- Structural domains involved in the regulation of transmitter release by synapsins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005Article
- Opposing changes in phosphorylation of specific sites in synapsin I during Ca2+-dependent glutamate release in isolated nerve terminals.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001Article
- Synapsin III: developmental expression, subcellular localization, and role in axon formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000Article
- Synapsins as regulators of neurotransmitter release.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 1999Review
- Synapsin I is structurally similar to ATP-utilizing enzymes.The EMBO journal · 1998Article
- Regulation of neuronal plasticity in the central nervous system by phosphorylation and dephosphorylation.Molecular neurobiology · 1998Review
- Identification, expression, and crystallization of the protease-resistant conserved domain of synapsin I.Protein science : a publication of the Protein Society · 1997Article
- The neurofilament antibody RT97 recognises a developmentally regulated phosphorylation epitope on microtubule-associated protein 1B.Journal of anatomy · 1997Article
- Glyceraldehyde-3-phosphate dehydrogenase activity and F-actin associations in synaptosomes and postsynaptic densities of porcine cerebral cortex.Cellular and molecular neurobiology · 1997Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synapsin I is a neuronal phosphoprotein comprised of two closely related polypeptides with apparent molecular weights of 78,000 and 76,000. It is found in association with the small vesicles clustered at the presynaptic junction. Its precise role is unknown, although it probably participates in vesicle clustering and/or release. Synapsin I is known to associate with vesicle membranes, microtubules, and neurofilaments. We have examined the interaction of purified phosphorylated and unphosphorylated bovine and human synapsin I with tubulin and actin filaments, using cosedimentation, viscometric, electrophoretic, and morphologic assays. As purified from brain homogenates, synapsin I decreases the steady-state viscosity of solutions containing F-actin, enhances the sedimentation of actin, and bundles actin filaments. Phosphorylation by cAMP-dependent kinase has minimal effect on this interaction, while phosphorylation by brain extracts or by purified calcium- and calmodulin-dependent kinase II reduces its actin-bundling and -binding activity. Synapsin's microtubule-binding activity, conversely, is stimulated after phosphorylation by the brain extract. Two complementary peptide fragments of synapsin generated by 2-nitro-5-thiocyanobenzoic cleavage and which map to opposite ends of the molecule participate in the bundling process, either by binding directly to actin or by binding to other synapsin I molecules. 2-Nitro-5-thiocyanobenzoic peptides arising from the central portion of the molecule demonstrate neither activity. In vivo, synapsin I may link small synaptic vesicles to the actin-based cortical cytoskeleton, and coordinate their availability for release in a Ca++-dependent fashion.
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