{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T05:25:20Z","timestamp":1788326720603,"version":"build-2803163510"},"reference-count":53,"publisher":"eLife Sciences Publications, Ltd","license":[{"start":{"date-parts":[[2023,1,17]],"date-time":"2023-01-17T00:00:00Z","timestamp":1673913600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2023,1,17]],"date-time":"2023-01-17T00:00:00Z","timestamp":1673913600000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2023,1,17]],"date-time":"2023-01-17T00:00:00Z","timestamp":1673913600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002428","name":"Austrian Science Fund","doi-asserted-by":"publisher","award":["P31813"],"award-info":[{"award-number":["P31813"]}],"id":[{"id":"10.13039\/501100002428","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002428","name":"Austrian Science Fund","doi-asserted-by":"publisher","award":["P31255-B27"],"award-info":[{"award-number":["P31255-B27"]}],"id":[{"id":"10.13039\/501100002428","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001821","name":"Vienna Science and Technology Fund","doi-asserted-by":"publisher","award":["LSC17-026"],"award-info":[{"award-number":["LSC17-026"]}],"id":[{"id":"10.13039\/501100001821","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elifesciences.org"],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2023,1,17]]},"abstract":"<jats:p>\n                    The serotonin transporter (SERT\/SLC6A4) is arguably the most extensively studied solute carrier (SLC). During its eponymous action \u2013 that is, the retrieval of serotonin from the extracellular space \u2013 SERT undergoes a conformational cycle. Typical inhibitors (antidepressant drugs and cocaine), partial and full substrates (amphetamines and their derivatives), and atypical inhibitors (ibogaine analogues) bind preferentially to different states in this cycle. This results in competitive or non-competitive transport inhibition. Here, we explored the action of\n                    <jats:italic>N<\/jats:italic>\n                    -formyl-1,3-bis (3,4-methylenedioxyphenyl)-prop-2-yl-amine (ECSI#6) on SERT: inhibition of serotonin uptake by ECSI#6 was enhanced with increasing serotonin concentration. Conversely, the K\n                    <jats:sub>M<\/jats:sub>\n                    for serotonin was lowered by augmenting ECSI#6. ECSI#6 bound with low affinity to the outward-facing state of SERT but with increased affinity to a potassium-bound state. Electrophysiological recordings showed that ECSI#6 preferentially interacted with the inward-facing state. Kinetic modeling recapitulated the experimental data and verified that uncompetitive inhibition arose from preferential binding of ECSI#6 to the K\n                    <jats:sup>+<\/jats:sup>\n                    -bound, inward-facing conformation of SERT. This binding mode predicted a pharmacochaperoning action of ECSI#6, which was confirmed by examining its effect on the folding-deficient mutant SERT-PG\n                    <jats:sup>601,602<\/jats:sup>\n                    AA: preincubation of HEK293 cells with ECSI#6 restored export of SERT-PG\n                    <jats:sup>601,602<\/jats:sup>\n                    AA from the endoplasmic reticulum and substrate transport. Similarly, in transgenic flies, the administration of ECSI#6 promoted the delivery of SERT-PG\n                    <jats:sup>601,602<\/jats:sup>\n                    AA to the presynaptic specialization of serotonergic neurons. To the best of our knowledge, ECSI#6 is the first example of an uncompetitive SLC inhibitor. Pharmacochaperones endowed with the binding mode of ECSI#6 are attractive, because they can rescue misfolded transporters at concentrations, which cause modest transport inhibition.\n                  <\/jats:p>","DOI":"10.7554\/elife.82641","type":"journal-article","created":{"date-parts":[[2023,1,17]],"date-time":"2023-01-17T10:00:47Z","timestamp":1673949647000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.82641","source":"Crossref","is-referenced-by-count":13,"title":["A mechanism of uncompetitive inhibition of the serotonin transporter"],"prefix":"10.7554","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7019-9180","authenticated-orcid":true,"given":"Shreyas","family":"Bhat","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03prydq77","id-type":"ROR","asserted-by":"publisher"}],"name":"Institute of Pharmacology and the Gaston H. 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