ArticleThe Journal of biological chemistry
Synaptophysin controls synaptobrevin-II retrieval via a cryptic C-terminal interaction site.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Increased Expression of α-Synuclein Impairs Trafficking of the Essential SNARE Protein Synaptobrevin-2.Journal of neurochemistry · 2026Article
- Synaptic vesicles that store monoamines and glutamate differ in protein composition.Science advances · 2026Article
- Synaptophysin autoantibodies mediate synaptic dysfunction in cerebellar ataxia.Cell reports. Medicine · 2026Article
- Biogenesis and reformation of synaptic vesicles.The Journal of physiology · 2025Review
- Article
- Indoxyl sulphate-TNFα axis mediates uremic encephalopathy in rodent acute kidney injury.Acta pharmacologica Sinica · 2024Article
- Possible role of lncRNAs in amelioration of Parkinson's disease symptoms by transplantation of dopaminergic cells.NPJ Parkinson's disease · 2024Article
- Inhibition of STAT3 signal pathway recovers postsynaptic plasticity to improve cognitive impairment caused by chronic intermittent hypoxia.Sleep & breathing = Schlaf & Atmung · 2023Article
- Article
- Room for Two: The Synaptophysin/Synaptobrevin Complex.Frontiers in synaptic neuroscience · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The accurate retrieval of synaptic vesicle (SV) proteins during endocytosis is essential for the maintenance of neurotransmission. Synaptophysin (Syp) and synaptobrevin-II (SybII) are the most abundant proteins on SVs. Neurons lacking Syp display defects in the activity-dependent retrieval of SybII and a general slowing of SV endocytosis. To determine the role of the cytoplasmic C terminus of Syp in the control of these two events, we performed molecular replacement studies in primary cultures of Syp knockout neurons using genetically encoded reporters of SV cargo trafficking at physiological temperatures. Under these conditions, we discovered, 1) no slowing in SV endocytosis in Syp knockout neurons, and 2) a continued defect in SybII retrieval in knockout neurons expressing a form of Syp lacking its C terminus. Sequential truncations of the Syp C-terminus revealed a cryptic interaction site for the SNARE motif of SybII that was concealed in the full-length form. This suggests that a conformational change within the Syp C terminus is key to permitting SybII binding and thus its accurate retrieval. Furthermore, this study reveals that the sole presynaptic role of Syp is the control of SybII retrieval, since no defect in SV endocytosis kinetics was observed at physiological temperatures.
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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.