C-terminal mutation induces a folding defect in the serotonin transporter

摘要: Neurotransmitter transporters are responsible for terminating signal transmission. hSERT (the human serotonin transporter) is the plasma membrane Na+/Cl--dependent transporter which uptake of from synaptic cleft. A previous study has shown that deleting C-terminus SERT impaired activity and compromised its delivery to membrane) [1]. However, this did not provide a mechanistic explanation. Alanine-scanning mutagenesis strategy was used in order delineate part required folding protein. Pairs alanine substitutions by site-directed have been produced we currently process testing effect these mutations on functional properties cellular localization SERT. The preliminary data show mutation P601G602-AA R607I608-AA (Sec24 binding site) causes intracellular retention abolishes binding.