Refine
Year of publication
- 2021 (232) (remove)
Document Type
- Preprint (232) (remove)
Language
- English (232)
Has Fulltext
- yes (232) (remove)
Is part of the Bibliography
- no (232)
Keywords
- 26 LncRNA (1)
- Acinetobacter baumannii (1)
- Amblyopia (1)
- BRAF (1)
- Bestattung (1)
- Binocular Rivalry (1)
- Brauchtum (1)
- Browsertool (1)
- Buparlisib (1)
- COVID-19 (1)
Institute
- Physik (143)
- Frankfurt Institute for Advanced Studies (FIAS) (118)
- Informatik (98)
- Medizin (32)
- Ernst Strüngmann Institut (7)
- Psychologie (7)
- Senckenbergische Naturforschende Gesellschaft (6)
- Buchmann Institut für Molekulare Lebenswissenschaften (BMLS) (5)
- Institut für Ökologie, Evolution und Diversität (5)
- MPI für Hirnforschung (5)
Release of neuropeptides from dense core vesicles (DCVs) is essential for neuromodulation. Compared to the release of small neurotransmitters, much less is known about the mechanisms and proteins contributing to neuropeptide release. By optogenetics, behavioral analysis, electrophysiology, electron microscopy, and live imaging, we show that synapsin SNN-1 is required for cAMP-dependent neuropeptide release in Caenorhabditis elegans hermaphrodite cholinergic motor neurons. In synapsin mutants, behaviors induced by the photoactivated adenylyl cyclase bPAC, which we previously showed to depend on acetylcholine and neuropeptides (Steuer Costa et al., 2017), are altered like in animals with reduced cAMP. Synapsin mutants have slight alterations in synaptic vesicle (SV) distribution, however, a defect in SV mobilization was apparent after channelrhodopsin-based photostimulation. DCVs were largely affected in snn-1 mutants: DCVs were ∼30% reduced in synaptic terminals, and not released following bPAC stimulation. Imaging axonal DCV trafficking, also in genome-engineered mutants in the serine-9 protein kinase A phosphorylation site, showed that synapsin captures DCVs at synapses, making them available for release. SNN-1 co-localized with immobile, captured DCVs. In synapsin deletion mutants, DCVs were more mobile and less likely to be caught at release sites, and in non-phosphorylatable SNN-1B(S9A) mutants, DCVs traffic less and accumulate, likely by enhanced SNN-1 dependent tethering. Our work establishes synapsin as a key mediator of neuropeptide release.
Based on electron-positron collision data collected with the BESIII detector operating at the BEPCII storage rings, the value of R≡σ(e+e−→hadrons)/σ(e+e−→μ+μ−) is measured at 14 center-of-mass energies from 2.2324 to 3.6710 GeV. The resulting uncertainties are less than 3.0%, and are dominated by systematic uncertainties.