25 research outputs found
5-HT2 receptors-mediated modulation of voltage-gated K+ channels and neurophysiopathological correlates
Gastrointestinal delivery of propofol from fospropofol: its bioavailability and activity in rodents and human volunteers
The effect of sevoflurane on glutamate release and uptake in rat cerebrocortical presynaptic terminals
A review of bipolarity concepts: history and examples from Radiolaria and Medusozoa (Cnidaria)
Depletion of the Ca++-dependent releasable pool of glutamate in striatal synaptosomes associated with dendrotoxin-induced potassium channel blockade
Isoflurane reduces synaptic glutamate release without changing cytosolic free calcium in isolated nerve terminals
HTDP-2, a New Synthetic Compound, Inhibits Glutamate Release through Reduction of Voltage-Dependent Ca2+ Influx in Rat Cerebral Cortex Nerve Terminals
Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis
Dynamin I is dephosphorylated at Ser-774 and Ser-778 during synaptic vesicle endocytosis (SVE) in nerve terminals. Phosphorylation was proposed to regulate the assembly of an endocytic protein complex with amphiphysin or endophilin. Instead, we found it recruits syndapin I for SVE and does not control amphiphysin or endophilin binding in rat synaptosomes. After depolarization, syndapin showed a calcineurin-mediated interaction with dynamin. A peptide mimicking the phosphorylation sites disrupted the dynamin-syndapin complex, not the dynamin-endophilin complex, arrested SVE and produced glutamate release fatigue after repetitive stimulation. Pseudophosphorylation of Ser-774 or Ser-778 inhibited syndapin binding without affecting amphiphysin recruitment. Site mutagenesis to alanine arrested SVE in cultured neurons. The effects of the sites were additive for syndapin I binding and SVE. Thus syndapin I is a central component of the endocytic protein complex for SVE via stimulus-dependent recruitment to dynamin I and has a key role in synaptic transmission