The cytoplasmic C2A domain of synaptotagmin shows sequence specific interaction with its own mRNA.

Synaptotagmin-1 (Syt1) is essential in Ca(2+)-dependent neurotransmitter release, but its expression regulation is unknown. Here we report that the cytoplasmic Syt1 fragment forms ribonucleoprotein complex by interacting with the 3' untranslated region (3(')UTR) of its own mRNA. Two protein-binding domains, GU(15) repeat and GUCAAUG, within the Syt 3'UTR and the C2 domains in Syt1, especially C2A, are essential in this ribonucleoprotein complex formation. Furthermore, in in vitro assay the translation efficiency of Syt1 mRNA was downregulated in presence of 3'UTR. These results demonstrate for the fist time that the soluble fraction of Syt1 can interact with its own mRNA in a highly sequence specific manner.