Attenuation of dopamine transporter activity by α-synuclein

@article{Wersinger2003AttenuationOD,
  title={Attenuation of dopamine transporter activity by $\alpha$-synuclein},
  author={Christophe Wersinger and Anita Sidhu},
  journal={Neuroscience Letters},
  year={2003},
  volume={340},
  pages={189-192}
}

α-Synuclein Stimulates a Dopamine Transporter-dependent Chloride Current and Modulates the Activity of the Transporter*

TLDR
Findings are consistent with the interpretation that DAT/α-synuclein interaction at the cell surface results in a DAT-dependent, Na+-insensitive, Cl-sensitive inward current with a decrease in substrate uptake, suggesting that Dat/ α-syn nuclein interaction can modulate dopamine transmission and thus neuronal function.

Inhibition of Vesicular Monoamine Transporter-2 Activity in α-Synuclein Stably Transfected SH-SY5Y Cells

TLDR
It is suggested that Up-regulated α-synuclein expression inhibits the activity of vesicular monoamine transporter-2, thereby interrupting dopamine homeostasis and resulting in dopaminergic neuron injury in Parkinson’s disease.

Modulation of dopamine transporter function by α‐synuclein is altered by impairment of cell adhesion and by induction of oxidative stress

TLDR
A novel normative role for α‐synuclein is suggested in regulating DA synaptic availability and homeostasis, which is relevant to the pathophysiology of PD.

Attenuation of the norepinephrine transporter activity and trafficking via interactions with α‐synuclein

TLDR
It is proposed that a primary physiological role of α‐Syn may be to regulate the homeostasis of monoamines in synapses, through modulatory interactions of the protein with monoaminergic transporters.

α-Synuclein and dopamine metabolism

TLDR
The regulatory effect of α-Syn on dopamine metabolism is likely to tone down the amount of cytoplasmic dopamine at nerve terminals, thereby limiting its conversion to highly reactive oxidative molecules.

Silencing α-Synuclein Gene Expression Enhances Tyrosine Hydroxylase Activity in MN9D Cells

TLDR
The data show that TH activity and DA biosynthesis were enhanced by down-regulation of α-synuclein, suggesting that α- synuclein may act as a negative regulator of cytosolic DA.

Striatal Dopamine Transporter Function Is Facilitated by Converging Biology of α-Synuclein and Cholesterol

TLDR
Data indicate that human α-synuclein in a mouse model of PD promotes striatal DAT function, in a manner supported by extracellular cholesterol, suggesting converging biology of α- synuclein and cholesterol that regulates DATfunction and could impact DA function and PD pathophysiology.
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