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The 'ins' and 'outs' of the high-affinity choline transporter CHT1
- Source :
- Journal of Neurochemistry. 97:1-12
- Publication Year :
- 2006
- Publisher :
- Wiley, 2006.
-
Abstract
- Maintenance of acetylcholine (ACh) synthesis depends on the activity of the high-affinity choline transporter (CHT1), which is responsible for the reuptake of choline from the synaptic cleft into presynaptic neurons. In this review, we discuss the current understanding of mechanisms involved in the cellular trafficking of CHT1. CHT1 protein is mainly found in intracellular organelles, such as endosomal compartments and synaptic vesicles. The presence of CHT1 at the plasma membrane is limited by rapid endocytosis of the transporter in clathrin-coated pits in a mechanism dependent on a dileucine-like motif present in the carboxyl-terminal region of the transporter. The intracellular pool of CHT1 appears to constitute a reserve pool of transporters, important for maintenance of cholinergic neurotransmission. However, the physiological basis of the presence of CHT1 in intracellular organelles is not fully understood. Current knowledge about CHT1 indicates that stimulated and constitutive exocytosis, in addition to endocytosis, will have major consequences for regulating choline uptake. Future investigations of CHT1 trafficking should elucidate such regulatory mechanisms, which may aid in understanding the pathophysiology of diseases that affect cholinergic neurons, such as Alzheimer's disease.
- Subjects :
- Synaptic cleft
Amino Acid Motifs
Presynaptic Terminals
Synaptic Membranes
Biology
Endocytosis
Synaptic Transmission
Biochemistry
Synaptic vesicle
Exocytosis
Reuptake
Cellular and Molecular Neuroscience
chemistry.chemical_compound
medicine
Animals
Humans
Neurotransmitter
Cation Transport Proteins
Acetylcholine
Cell biology
Choline transporter
Protein Transport
chemistry
Neuroscience
medicine.drug
Subjects
Details
- ISSN :
- 14714159 and 00223042
- Volume :
- 97
- Database :
- OpenAIRE
- Journal :
- Journal of Neurochemistry
- Accession number :
- edsair.doi.dedup.....380b2d1c0125adf0113a4aafb22e0141