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Related Experiment Video

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Brain Slice Biotinylation: An Ex Vivo Approach to Measure Region-specific Plasma Membrane Protein Trafficking in Adult Neurons

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Synucleins antagonize endoplasmic reticulum function to modulate dopamine transporter trafficking.

Adam W Oaks¹, Nicholas Marsh-Armstrong, Jessica M Jones

¹Laboratory of Molecular Neurochemistry, Department of Biochemistry and Molecular & Cellular Biology, Georgetown University Medical Center, Washington, DC, USA.

|August 23, 2013

Summary

All three synuclein proteins negatively regulate dopamine transporter (DAT) cell surface levels by impairing ER-Golgi transport. This finding reveals a new role for synucleins in protein trafficking via the secretory pathway.

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Area of Science:

Neuroscience
Cell Biology
Molecular Biology

Background:

Dopamine transporter (DAT) surface levels control dopamine reuptake.
Alpha-synuclein, linked to Parkinson's disease, modulates DAT trafficking.
The roles of beta- and gamma-synuclein in DAT trafficking are unknown.

Purpose of the Study:

To investigate the impact of beta- and gamma-synuclein on DAT trafficking.
To elucidate the mechanism by which synucleins affect DAT cell surface distribution.

Main Methods:

Utilized SH-SY5Y cells as a model system for DAT trafficking studies.
Examined the effects of alpha-, beta-, and gamma-synuclein on DAT localization.
Assessed the impact of synucleins on the endoplasmic reticulum (ER) to Golgi transition.

Main Results:

All three synuclein proteins (alpha, beta, and gamma) were found to negatively regulate DAT cell surface distribution.
Synucleins were shown to limit DAT export from the ER.
Impairment of the ER-Golgi transition by synucleins leads to DAT accumulation in the ER.

Conclusions:

The extended synuclein family plays a significant role in regulating DAT trafficking.
Synucleins influence DAT export by affecting ER and Golgi function.
This mechanism highlights a previously unappreciated role for synucleins in secretory pathway-dependent protein trafficking.