Synapsin III and alpha-Synuclein

Author: Gianpiero Pescarmona
Date: 02/09/2018


Synapsin cartoons:

The dopaminergic terminal with and without α-syn. (A) Putative organization of a presynaptic dopamine (DA) terminal under physiological conditions. (B) The absence of α-syn decreases the amount of membrane DAT and increases the density of synapsin III in presynaptic boutons, thus altering the proper clustering of synaptic vesicles at the active zone. This coincides with a reduction of dopamine release. © Aggregation of α-syn might determine a rearrangement of dopamine terminals, similar to its absence. A marked reduction of DAT, a significant accumulation of synapsin III and a collapse of synaptic vesicle pools coinciding with the reduction of their clustering at the active zone could reduce dopamine release.


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α-synuclein and synapsin III cooperatively regulate synaptic function in dopamine neurons, 2018

  • The main neuropathological features of Parkinson's disease are dopaminergic nigrostriatal neuron degeneration, and intraneuronal and intraneuritic proteinaceous inclusions named Lewy bodies and Lewy neurites, respectively, which mainly contain α-synuclein (α-syn, also known as SNCA). The neuronal phosphoprotein synapsin III (also known as SYN3), is a pivotal regulator of dopamine neuron synaptic function. Here, we show that α-syn interacts with and modulates synapsin III. The absence of α-syn causes a selective increase and redistribution of synapsin III, and changes the organization of synaptic vesicle pools in dopamine neurons. In α-syn-null mice, the alterations of synapsin III induce an increased locomotor response to the stimulation of synapsin-dependent dopamine overflow, despite this, these mice show decreased basal and depolarization-dependent striatal dopamine release. Of note, synapsin III seems to be involved in α-syn aggregation, which also coaxes its increase and redistribution. Furthermore, synapsin III accumulates in the caudate and putamen of individuals with Parkinson's disease. These findings support a reciprocal modulatory interaction of α-syn and synapsin III in the regulation of dopamine neuron synaptic function.

Sweet insights into learning and memory, 2006

  • Studies have linked the Fucα(1-2)Gal modification of neuronal glycoproteins to cognitive processes such as learning and memory. The identification of synapsins Ia and Ib as the main Fucα(1-2)Gal-bearing neuronal proteins not only suggests previously unknown molecular mechanisms of neuronal plasticity but also indicates the existence of previously unknown glycosylation pathways in neurons.
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Identification of a highly neurotoxic α-synuclein species inducing mitochondrial damage and mitophagy in Parkinson’s disease, 2018

  • Parkinson’s disease (PD) is a neurodegenerative disease linked to the misfolding and aggregation of a protein called “α-synuclein.” α-Synuclein aggregates found in the brains of PD patients are called “Lewy bodies” and “Lewy neurites.” We discovered the existence of a type of α-synuclein aggregate, smaller than previously described and conformationally distinct, that we called “pα-syn*.” Pα-syn* was present in neuronal cultures and mice brains injected with recombinant α-synuclein fibrils as well as in the brains of PD patients. We showed that pα-syn* is made of trimmed α-synuclein resulting from a failed cellular attempt to degrade fibrillar α-synuclein aggregates. We found that pα-syn* is a major neurotoxic species inducing mitochondrial damage, fission, and mitophagy, therefore constituting a central player in PD pathogenesis.

Form and Function: What Makes α-Synuclein Toxic? 2015


2018-09-25T09:58:14 - Gianpiero Pescarmona

Valine transport

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