Journal
JOURNAL OF CHEMICAL NEUROANATOMY
Volume 83, Issue -, Pages 3-9Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jchemneu.2017.01.002
Keywords
Posttranslational modification; Palmitoyl acyl transferase; Acyl protein thioesterase; Phosphorylation; Protein trafficking; 2 Bromopalmitate
Categories
Funding
- National Institutes of Health [DA 031991, DA13147, 5P20-104360, P30-GM103329, P20-GM12345]
- ND EPSCoR Doctoral Dissertation Fellowship
Ask authors/readers for more resources
The neurotransmitter dopamine (DA) plays a key role in several biological processes including reward, mood, motor activity and attention. Synaptic DA homeostasis is controlled by the dopamine transporter (DAT) which transports extracellular DA into the presynaptic neuron after release and regulates its availability to receptors. Many neurological disorders such as schizophrenia, bipolar disorder, Parkinson disease and attention-deficit hyperactivity disorder are associated with imbalances in DA homeostasis that may be related to DAT dysfunction. DAT is also a target of psychostimulant and therapeutic drugs that inhibit DA reuptake and lead to elevated dopaminergic neurotransmission. We have recently demonstrated the acute and chronic modulation of DA reuptake activity and DAT stability through Spalmitoylation, the linkage of a 16-carbon palmitate group to cysteine via a thioester bond. This review summarizes the properties and regulation of DAT palmitoylation and describes how it serves to affect various transporter functions. Better understanding of the role of palmitoylation in regulation of DAT function may lead to identification of therapeutic targets for modulation of DA homeostasis in the treatment of dopaminergic disorders. (C) 2017 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available