RT Conference Proceedings
T1 SYT6 protein role in Arabidopsis thaliana contact sites.
A1 Moya-Barrientos, Miriam
A1 Huércano Rubens, Carolina
A1 Morello-López, Jorge
A1 Cardeñas Echevarría, Carlos
A1 Boutté, Yohann
A1 Sánchez-Vera, Victoria
A1 Ruiz-López, Noemí
K1 Arabidopsis thaliana - Citología
K1 Proteínas vegetales
AB The SYT6 protein from A. thaliana (AT3G18370) has recently been identified as a lipid transfer protein localized at membrane contact sites (MCS). MCS are regions where membranes of two organelles closely approach without membrane fusing, typically within 10-30 nm [1]. Historically, research has primarily focused on endoplasmic reticulum (ER) and plasma membrane (PM) MCS [2], but recently MCS involving the ER and other organelles have come to light. SYT6 is a plant exclusive protein exhibiting a modular structure shared with mammalian Extended-Synaptotagmins (E-SYTs) and other plant synaptotagmins, such as SYT1. Our ongoing experiments suggest that SYT6 anchors itself to the ER via its transmembrane domain (TM), contains a lipid trafficking domain (named SMP) [3] and attaches to specific trans-Golgi Network (TGN) vesicles through its C2 domains and coiled-coil domain. These observations make SYT6 a particularly intriguing protein, given that its physiological roles remain unclear. Currently, our focus lies in studying SYT6 to uncover its expression, subcellular localization and most importantly, its function. Thanks to confocal imaging, we have confirmed SYT6 attachment to the ER and to big and small vesicles in continuous motion, suggesting its involvement in secretory trafficking. These findings, combined with Co-Immunoprecipitation experiments, have confirmed the interaction between SYT6 and specific TGN proteins linked to the independent Golgi TGN (GI-TGN). Moreover, our preliminary findings have showed a correlation between SYT6, exocytosis and autophagy. Furthermore, it has been observed that syt6 mutant exhibits distinct phenotypic traits compared to the wild-type, notably displaying altered negative gravitropism. Altogether, these findings suggest that SYT6 represents a novel ER-TGN CS protein that may play a role in secretory trafficking.
YR 2024
FD 2024
LK https://hdl.handle.net/10630/31770
UL https://hdl.handle.net/10630/31770
LA eng
NO This work has been funded by grant PID2021-127649OB-I00 (by MCIN/AEI/ 10.13039/501100011033 and by the European Union), Ayuda D2 Plan Propio by Universidad de Málaga and Proyecto QUAL21 012 IHSM (Consejería de Universidad, Investigación e Innovación, Junta de Andalucía). Universidad de Málaga. Campus de Excelencia Internacional Andalucía Tech.
DS RIUMA. Repositorio Institucional de la Universidad de Málaga
RD 20 ene 2026