Editing Vesicular monoamine transporter (section)

===Clinical research===
Genetic research models have shown that polymorphisms in ''SLC18A1'' and ''SLC18A2'', the genes that encode for VMAT1 and 2 proteins, respectively, may confer risk for some neuropsychiatric disorders;<ref name="Wimalasena, K. 2011"/><ref name="Glatt CE, Wahner AD, White DJ, Ruiz-Linares A, Ritz B 2006 299–305"/><ref name="Lawal HO 2013">{{cite journal |vauthors=Lawal HO, Krantz DE | year = 2013 | title = SLC18: Vesicular neurotransmitter transporters for monoamines and acetylcholine | journal = Molecular Aspects of Medicine | volume = 34 | issue = 2–3| pages = 360–372 | doi = 10.1016/j.mam.2012.07.005 | pmid=23506877 | pmc=3727660}}</ref> however, no specific diseases have been identified yet as directly resulting from a genetic mutation in an ''SLC18'' gene, which codes for VMAT proteins.<ref name="Lawal HO 2013"/>

Much of the current research related to VMAT explores the genetic underpinnings of neuropsychiatric disorders as they may be affected by ''SLC18A'' family mutations.

The dopaminergic neuron is known to play a central role in drug addiction and abuse and the potential role of the dopamine transporter has been well-explored as a target for amphetamine and cocaine. Current research looks toward VMAT2 as a target for such psychostimulants. A combination of imaging, neurochemical, biochemical, cell biological, genetic, and immunohistochemical evidence has been compiled to provide the most current comprehensive understanding of the role the VMAT2 plays in amphetamine and cocaine abuse and addiction through aminergic neurotransmission.<ref name="E Weihe" /><ref name="Lawal HO 2013"/>

As VMATs are membrane proteins, structural information is limited and researchers have yet to completely understand the structure of both isoforms. Further studies are needed in order to determine the structure and therefore complete function of these proteins. There is preliminary evidence that the gene for VMAT1 may be linked to susceptibility to [[schizophrenia]], [[bipolar disorder]], and various anxiety disorders.<ref name="Wimalasena, K. 2011"/> Further studies are needed in order to confirm these findings and to gain a better understanding of the role of VMATs in the central nervous system.

Multiple [[single-nucleotide polymorphism]]s (SNPs) have been identified in the [[coding region]] of VMATs. The effects of some of these SNPs have been alteration of VMAT function, structure and regulation.<ref name = "sager">Sager, J.J. & Torres, G.E., 2011. Proteins interacting with monoamine transporters: Current state and future challenges. Biochemistry, [online] Available at: <http://pubs.acs.org/doi/ipdf/10.1021/bi200405c>[Accessed 20 April 2013]</ref> Further investigation of these SNPs is required in order to distinguish whether they may be attributable to certain diseases with suspected SNP-[[mutation]] origins.

α-synuclein, a cytosolic protein found mainly in [[chemical synapse|pre-synaptic]] nerve terminals, has been found to have regulatory interactions with the trafficking of VMATs; mutations involving α-synuclein have been linked to familial PD.<ref name = "sager"/> Further research is needed to clarify the extent to which these proteins modulate the trafficking of VMATs, and whether they may be exploited in order to gather more information about the exact mechanism of how disorders such as PD occurs, and how they may potentially be treated.

Studies have shown that at the synaptic membrane, [[enzyme]]s responsible for the synthesis of dopamine, [[tyrosine hydroxylase]] and amino acid aromatic decarboxylase are physically and functionally coupled with VMAT2.<ref name="sager"/> It was initially thought that the synthesis of these substances and the subsequent packaging of them into vesicles were two entirely separate processes.