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

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dc.contributorSukumaran, Sunitha S.
dc.contributorBanerjee, Siddharth
dc.contributorBhasker, Salini
dc.contributorThekkuveettil, Anoopkumar
dc.date.accessioned2012-12-04T11:45:31Z
dc.date.available2012-12-04T11:45:31Z
dc.date.issued2008
dc.description.abstractSynaptotagmin-1 (Syt1) is essential in Ca2+-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. (C) 2008 Elsevier Inc All rights reserved.
dc.identifier.citationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. 373; 4; 509-514en_US
dc.identifier.urihttp://dx.doi.org/10.1016/j.bbrc.2008.06.063
dc.identifier.urihttps://dspace.sctimst.ac.in/handle/123456789/1190
dc.publisherBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
dc.subjectBiochemistry
dc.titleThe cytoplasmic C2A domain of synaptotagmin shows sequence specific interaction with its own mRNA
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