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dc.contributor.authorRuiz López, Noemi
dc.contributor.authorPérez Sancho, Jessica
dc.contributor.authorEsteban del Valle, Alicia
dc.contributor.authorGarcía Hernández, Selene
dc.contributor.authorHuércano Rubens, Carolina
dc.contributor.authorPercio Vargas, Francisco
dc.contributor.authorBenitez de la Fuente, Francisco
dc.contributor.authorOsorio-Algar, Sonia 
dc.contributor.authorSteffen, Vanneste
dc.contributor.authorLothar, Willmitzer
dc.contributor.authorNapier, Johnathan A.
dc.contributor.authorPerea, Carlos
dc.contributor.authorSalinas, Julio
dc.contributor.authorAmorim-Silva, Vitor
dc.contributor.authorBotella-Mesa, Miguel Angel
dc.date.accessioned2019-11-13T09:32:27Z
dc.date.available2019-11-13T09:32:27Z
dc.date.created2019
dc.date.issued2019-11-13
dc.identifier.urihttps://hdl.handle.net/10630/18764
dc.description.abstractBulk 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.en_US
dc.description.sponsorshipUniversidad de Málaga. Campus de Excelencia Internacional Andalucía Tech. The authors acknowledge the support by the Plan Propio from University of Malaga, Campus de Excelencia 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.en_US
dc.language.isoengen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectLípidosen_US
dc.subject.otherDiacylglycerolen_US
dc.subject.otherContact sitesen_US
dc.subject.otherAbiotic stressen_US
dc.subject.otherLipid signallingen_US
dc.titleDiacylglycerol transport by Arabidopsis Synaptotagmin 1 at ERplasma membrane contact sites under abiotic stress.en_US
dc.typeinfo:eu-repo/semantics/conferenceObjecten_US
dc.centroFacultad de Cienciasen_US
dc.relation.eventtitleSmall Molecules in Plan Research, 2019en_US
dc.relation.eventplaceValencia, Españaen_US
dc.relation.eventdate10-11 diciembre 2019en_US


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