RT Conference Proceedings
T1 Diacylglycerol transport by Arabidopsis Synaptotagmin 1 at ERplasma membrane contact sites under abiotic stress.
A1 Ruiz-López, Noemí
A1 Pérez-Sancho, Jessica
A1 Esteban del Valle, Alicia
A1 García-Hernández, Selene
A1 Huércano Rubens, Carolina
A1 Percio-Vargas, Francisco
A1 Benítez de la Fuente, Francisco
A1 Osorio-Algar, Sonia
A1 Steffen, Vanneste
A1 Lothar, Willmitzer
A1 Napier, Johnathan A.
A1 Perea, Carlos
A1 Salinas, Julio
A1 Amorim-Silva, Vitor
A1 Botella-Mesa, Miguel Ángel
K1 Lípidos
AB Bulk lipid transport between membranes within cells involves vesicles, however membrane contact sites have recently been discovered as mediators of non-vesicular lipid transfer. ER-PM contact sites are conserved structures defined as regions of the endoplasmic reticulum (ER) that tightly associate with the plasma membrane (PM). Our recent data suggest that the constitutively expressed Arabidopsis Synaptotagmin 1 (SYT1) and the cold-induced homolog AtSYT3 are proteins located in these ER-PM contact sites that are essential for the tolerance various abiotic stresses. Arabidopsis SYTs proteins are integral membrane proteins that contain multiple Ca2+-binding C2 domains and a synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain that contains a hydrophobic groove. In mammals, several SMP proteins are responsible for the inter-organelle transport of glycerophospholipids. Our experiments have demonstrated that there is a recruitment of AtSYT1 and AtSTYT3 to ER-PM contact sites under stress conditions and it requires phosphatidylinositol 4- phosphate, PI(4)P in the PM, in opposition to the recruitment of PI(4,5)P2 in mammals. Moreover, our recent high-resolution lipidome analysis suggest that saturated diacylglycerols (DAGs) are the lipids that AtSYT1 is transferring between the PM and ER. Additionally, we have identified AtDGK2 (diacylglycerol kinase 2) as a key interactor of AtSYT1. Generally, in response to a stress stimulus, a phospholipase C (PLC), hydrolyses PIP2 after the elevation of cytosolic Ca2+, generating DAGs which immediately can be converted to phosphatidic acid (PA) by DGKs.
YR 2019
FD 2019-11-13
LK https://hdl.handle.net/10630/18764
UL https://hdl.handle.net/10630/18764
LA eng
NO Universidad de Málaga. Campus de Excelencia Internacional Andalucía Tech.The authors acknowledge the support by the Plan Propio from University of Malaga, Campus deExcelencia Internacional de Andalucía and by the Redes of Excelencia (BIO2014-56153-REDT) and BIO2017-82609-R, RYC-2016-21172 & PGC2018-098789 of the Ministerio de Economía, Industria y Competitividad.
DS RIUMA. Repositorio Institucional de la Universidad de Málaga
RD 20 ene 2026