Consideration of allosterism and interacting proteins in the physiological functions of the serotonin transporter
Biochemical Pharmacology, ISSN: 0006-2952, Vol: 83, Issue: 4, Page: 435-442
2012
- 23Citations
- 49Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations23
- Citation Indexes23
- 23
- CrossRef17
- Captures49
- Readers49
- 49
Article Description
The serotonin transporter (SERT) functions to transport serotonin (5-HT) from the extracellular space into neurons to maintain homeostatic control of 5-HT. It is the molecular target for selective serotonin reuptake inhibitor (SSRI) antidepressants. Preclinical research has shown that some SERT inhibitors can bind to two distinct binding sites on the SERT, a primary high affinity binding site and a low affinity allosteric binding site. Mutational studies of the SERT and computational modeling methods with escitalopram resulted in the identification of key amino acid residues important for the function of the allosteric binding site. While this allosteric binding site appears to influence the clinical efficacy of escitalopram under physiological conditions, the molecular mechanism of this effect is still poorly understood and may involve a large network of protein–protein interactions with the SERT. Dynamic interfaces between the SERT and the SERT interacting proteins (SIPs) potentially influence not only the SERT on its uptake function, its regulation, and trafficking, but also on known as well as yet to be identified non-canonical signaling pathways through SIPs. In this commentary, we outline approaches in the areas of selective small-molecule allosteric compound discovery, biochemistry, in vivo genetic knock-in mouse models, as well as computational and structural biology. These studies of the intra-molecular allosteric modulation of the SERT in the context of the myriad of potential inter-molecular signaling interactions with SIPs may help uncover unknown physiological functions of the SERT.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006295211007003; http://dx.doi.org/10.1016/j.bcp.2011.09.020; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84855759792&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/21983034; https://linkinghub.elsevier.com/retrieve/pii/S0006295211007003; https://dx.doi.org/10.1016/j.bcp.2011.09.020
Elsevier BV
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