ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2002
Accessibility and conformational coupling in serotonin transporter predicted internal domains.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 82 citations in OpenAlex.
- Determining Ligand and Ion-Induced Conformational Changes in Serotonin Transporter with Its Fluorescent Substrates.International journal of molecular sciences · 2022Article
- Sodium Binding Stabilizes the Outward-Open State of SERT by Limiting Bundle Domain Motions.Cells · 2022Article
- Serotonin Transporter Ala276 Mouse: Novel Model to Assess the Neurochemical and Behavioral Impact of Thr276 Phosphorylation In Vivo.Neurochemical research · 2022Review
- Using CaPsychopharmacology · 2019Review
- A Single Pair of Serotonergic Neurons Counteracts Serotonergic Inhibition of Ethanol Attraction in Drosophila.PloS one · 2016Article
- A dualistic conformational response to substrate binding in the human serotonin transporter reveals a high affinity state for serotonin.The Journal of biological chemistry · 2015Article
- Structure and regulatory interactions of the cytoplasmic terminal domains of serotonin transporter.Biochemistry · 2014Article
- The two Na+ sites in the human serotonin transporter play distinct roles in the ion coupling and electrogenicity of transport.The Journal of biological chemistry · 2014Article
- Cocaine self-administration produces pharmacodynamic tolerance: differential effects on the potency of dopamine transporter blockers, releasers, and methylphenidate.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2012Article
- Cytoplasmic permeation pathway of neurotransmitter transporters.Biochemistry · 2011Review
- Structural analysis of the extracellular entrance to the serotonin transporter permeation pathway.The Journal of biological chemistry · 2010Article
- Transmembrane domain 6 of the human serotonin transporter contributes to an aqueously accessible binding pocket for serotonin and the psychostimulant 3,4-methylene dioxymethamphetamine.The Journal of biological chemistry · 2010Article
- Interaction of catechol and non-catechol substrates with externally or internally facing dopamine transporters.Journal of neurochemistry · 2009Article
- A closer look at amphetamine-induced reverse transport and trafficking of the dopamine and norepinephrine transporters.Molecular neurobiology · 2009Review
- Article
- Mechanism for alternating access in neurotransmitter transporters.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Involvement of serotonin transporter extracellular loop 1 in serotonin binding and transport.Molecular membrane biology · 2008Article
- Serotonin transporter phosphorylation by cGMP-dependent protein kinase is altered by a mutation associated with obsessive compulsive disorder.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- Three ubiquitin conjugation sites in the amino terminus of the dopamine transporter mediate protein kinase C-dependent endocytosis of the transporter.Molecular biology of the cell · 2007Article
- Serotonin transporters--structure and function.The Journal of membrane biology · 2006Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intracellular topology of serotonin transporter (SERT) was examined using mutants containing single cysteine residues in the predicted cytoplasmic domain of the protein. Cysteine residues in each predicted cytoplasmic domain, including the NH2 and COOH termini and the five predicted internal loops, reacted with methanethiosulfonate (MTS) reagents only when the plasma membrane was permeabilized with digitonin or in membrane preparations but not in intact cells. The reaction was monitored by inactivation of high-affinity binding activity and by incorporation of biotin groups into the protein. Of the seven endogenous cysteine residues predicted to lie in the cytoplasmic domain, modification of only Cys-357 in the third internal loop (IL3) led to loss of activity. Cys-15 in the NH2 terminus and Cys-622 in the COOH terminus also reacted with MTS reagents. Modification of cysteine residues inserted at positions 137 in IL1, 277 in IL2, and 441 in IL4 also led to inactivation, and at positions 157 in IL1 and 532 in IL5, cysteine was modified without an effect on binding activity. These results are in agreement with the originally proposed topology for SERT and argue against an alternative topology proposed for the closely related GABA and glycine transporters. The reactivity of many of the cytoplasmic cysteine residues studied was influenced by ion and ligand binding, suggesting that the internal domains of SERT participate in conformational changes during neurotransmitter transport.
Indexed as
Identifiers
12351711PMC6757799W2122565898What OpenQuestion holds
Registered trials
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