<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-05-31T13:19:05Z</responseDate><request verb="GetRecord" identifier="oai:riuma.uma.es:10630/35583" metadataPrefix="oai_dc">https://riuma.uma.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:riuma.uma.es:10630/35583</identifier><datestamp>2026-04-10T08:28:22Z</datestamp><setSpec>com_10630_2254</setSpec><setSpec>col_10630_37959</setSpec></header><metadata><oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:doc="http://www.lyncode.com/xoai" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
   <dc:title>Characterizing SYT6, a lipid transfer protein at the secretory pathway.</dc:title>
   <dc:creator>Moya-Barrientos, Miriam</dc:creator>
   <dc:creator>Huércano Rubens, Carolina</dc:creator>
   <dc:creator>Morello-López, Jorge</dc:creator>
   <dc:creator>Cardeñas Echevarría, Carlos</dc:creator>
   <dc:creator>Boutté, Yohann</dc:creator>
   <dc:creator>Sánchez-Vera, Victoria</dc:creator>
   <dc:creator>Ruiz-López, Noemí</dc:creator>
   <dc:subject>Arabidopsis thaliana</dc:subject>
   <dc:subject>SYT6</dc:subject>
   <dc:subject>ER</dc:subject>
   <dc:subject>TGN</dc:subject>
   <dc:description>The SYT6 protein from A. thaliana has recently been identified as a lipid transfer &#xd;
protein localized at membrane contact sites (MCS). MCS are regions where &#xd;
membranes of two organelles closely approach without membrane fusing. Historically, &#xd;
research has focused on endoplasmic reticulum (ER) and plasma membrane MCS, &#xd;
but recently MCS involving the ER and other organelles have come to light. SYT6 is a &#xd;
plant-exclusive protein exhibiting a modular structure shared with mammalian &#xd;
Extended-Synaptotagmins and other plant synaptotagmins, such as SYT1.  &#xd;
Our ongoing experiments suggest that SYT6 anchors itself to the ER via its &#xd;
transmembrane domain, contains a lipid trafficking domain (named SMP) and attaches &#xd;
to specific trans-Golgi Network (TGN) vesicles through its C2 domains and coiled-coil &#xd;
domain. These observations make SYT6 particularly intriguing, as its physiological &#xd;
roles remain unclear.  &#xd;
Currently, our focus is on studying SYT6 to uncover its expression, subcellular &#xd;
localization and most importantly, its function. Confocal imaging, has confirmed SYT6 &#xd;
attachment to the ER and to vesicles in continuous motion, suggesting involvement in &#xd;
secretory trafficking. Co-Immunoprecipitation and BiFC experiments, have confirmed &#xd;
the interaction between SYT6 and specific TGN proteins linked to the independent &#xd;
Golgi TGN (GI-TGN). Preliminary findings indicate a correlation between SYT6, and &#xd;
exocytosis. Furthermore, syt6 mutant displays altered negative gravitropism. &#xd;
Altogether, these findings suggest that SYT6 represents a novel ER-TGN CS protein &#xd;
that may play a role in secretory trafficking.</dc:description>
   <dc:description>This work has been funded by grant PID2021-127649OB-I00 (by &#xd;
MCIN/AEI/ 10.13039/501100011033 and by the European Union), Ayuda D2 Plan &#xd;
Propio by Universidad de Málaga and Proyecto QUAL21 012 IHSM (Consejería de &#xd;
Universidad, Investigación e Innovación, Junta de Andalucía).</dc:description>
   <dc:date>2024-12-11T10:15:05Z</dc:date>
   <dc:date>2024-12-11T10:15:05Z</dc:date>
   <dc:date>2024</dc:date>
   <dc:type>conference output</dc:type>
   <dc:identifier>https://hdl.handle.net/10630/35583</dc:identifier>
   <dc:language>eng</dc:language>
   <dc:relation>2024 International Symposium on Plant Lipids (ISPL 2024)</dc:relation>
   <dc:relation>Lincoln, Nebraska Estados Unidos</dc:relation>
   <dc:relation>julio de 2024</dc:relation>
   <dc:rights>open access</dc:rights>
   <dc:format>application/pdf</dc:format>
</oai_dc:dc>
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