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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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Substrate-induced internalization of the high-affinity choline transporter.

Takashi Okuda¹, Asami Konishi, Hidemi Misawa

¹Department of Pharmacology, Faculty of Pharmacy, Keio University, Minato-ku, Tokyo 105-8512, Japan. okuda-tk@pha.keio.ac.jp

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience

|October 22, 2011

Summary

Extracellular choline reduces cell-surface expression of the high-affinity choline transporter (CHT1) by accelerating its internalization. This provides a novel feedback mechanism regulating acetylcholine synthesis in cholinergic neurons.

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Area of Science:

Neuroscience
Cell Biology
Neurochemistry

Background:

Cholinergic neurons synthesize acetylcholine (ACh) via high-affinity choline uptake.
The high-affinity choline transporter 1 (CHT1) mediates this rate-limiting step.
Factors regulating CHT1 expression and function remain largely unknown.

Purpose of the Study:

To investigate endogenous factors affecting CHT1 cell-surface expression and function.
To elucidate the regulatory mechanisms of acetylcholine synthesis.

Main Methods:

Experiments using rat brain synaptosomes and primary basal forebrain cultures.
Mammalian cell lines (HEK293) transfected with CHT1.
Investigated effects of extracellular substrate, pH, and hemicholinium-3 on CHT1 internalization and surface expression.

Main Results:

Extracellular substrate (choline) decreases cell-surface CHT1 expression by promoting its internalization.
This internalization is mediated by a dynamin-dependent endocytosis pathway.
The CHT1 inhibitor hemicholinium-3 reduces constitutive internalization, increasing surface expression.
Constitutive CHT1 internalization is dependent on extracellular pH.

Conclusions:

Extracellular substrate induces CHT1 internalization, establishing a novel feedback loop.
This mechanism regulates acetylcholine synthesis at cholinergic presynaptic terminals.