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Background The serotonin transporter (SERT) belongs to the SLC6 family of neurotransmitter transporters, which mediate reuptake of previously released neurotransmitters from the synapse. Mutation of C-terminus residues RI607– 608 to alanine results in intracellular retention of SERT [1]. We subsequently showed that SERT depends on the COPII component SEC24C for its ER export and proposed RI607–608 as a putative interaction site on SERT for SEC24 proteins [2]. The aim of our current study is to characterise the nature of ER export of monoamine transporters.

Characterising the interaction between the COPII component SEC24C and the human serotonin transporter