Characterising the interaction between the COPII component SEC24C and the human serotonin transporter
نویسندگان
چکیده
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.
منابع مشابه
The Serotonin Transporter Is an Exclusive Client of the Coat Protein Complex II (COPII) Component SEC24C*
The transporters for serotonin (SERT), dopamine, and noradrenaline have a conserved hydrophobic core but divergent N and C termini. The C terminus harbors the binding site for the coat protein complex II (COPII) cargo-binding protein SEC24. Here we explored which SEC24 isoform was required for export of SERT from the endoplasmic reticulum (ER). Three lines of evidence argue that SERT can only e...
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Export of the serotonin transporter (SERT) from the endoplasmic reticulum (ER) is mediated by the SEC24C isoform of the coatomer protein-II complex. SERT must enter the axonal compartment and reach the presynaptic specialization to perform its function, i.e., the inward transport of serotonin. Refilling of vesicles is contingent on the operation of an efficient relay between SERT and the vesicu...
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Secretory proteins are exported from the endoplasmic reticulum in COPII vesicles. SNARE proteins-core machinery for membrane fusion-are incorporated into COPII vesicles by direct interaction with Sec24. Here we report a novel mechanism for sorting of the ER-Golgi Q-SNAREs into COPII vesicles. Different mammalian Sec24 isoforms recruit either the R-SNARE Sec22b or the Q-SNAREs Syntaxin5, GS27, a...
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