AI Article Synopsis
- - Synaptotagmin-1 (Syt1) is crucial for the release of neurotransmitters that depend on calcium ions, but how its expression is regulated is unclear.
- - The study finds that a fragment of Syt1 interacts with the 3' untranslated region (3'UTR) of its own mRNA, forming a ribonucleoprotein complex.
- - Key protein-binding domains in Syt1's mRNA and specific regions within Syt1 are necessary for this interaction, which ultimately reduces the translation efficiency of Syt1 mRNA.
Article Abstract
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.
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| http://dx.doi.org/10.1016/j.bbrc.2008.06.063 | DOI Listing |
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