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dc.contributor.authorHuércano Rubens, Carolina
dc.contributor.authorPercio Vargas, Francisco
dc.contributor.authorSánchez-Vera, Victoria
dc.contributor.authorMorello-López, Jorge
dc.contributor.authorBotella-Mesa, Miguel Angel 
dc.contributor.authorRuiz López, Noemi
dc.date.accessioned2021-07-13T11:28:42Z
dc.date.available2021-07-13T11:28:42Z
dc.date.created2021
dc.date.issued2021
dc.identifier.urihttps://hdl.handle.net/10630/22639
dc.description.abstractMembrane contact sites (MCS) are microdomains where two membranes of two different organelles are in close apposition, but they do not fuse. MCS are essential for non-vesicular transport of lipids. This lipid transport is mediated by several families of proteins which all of them contain a lipid transport domain, as the synaptotagmin-like mitochondrial lipid-binding (SMP) domain. The most studied SMP protein is Arabidopsis SYT1 which is known to be involved in tolerance to multiple abiotic stresses. Later studies in other SMP proteins of the same family have shown that SYT1 and homologous such as SYT3 or SYT5 gave similar results. However, little information is available about the role other SMP proteins in plants. We have studied the occurrence of additional SMP proteins in A. thaliana and S. lycopersicum. In order to identify these proteins, SMP sequences from human and yeast were used to identify their remote orthologues in A. thaliana and S. lycopersicum, allowing the identification of several putative encoding SMP domains. We have found that some of the identified proteins are exclusive of plants as they do not have direct orthologs in yeast nor human. Transient expression in N. benthamiana leaves followed by confocal microscopy was used to study the subcellular localization of these proteins. Our results show that some of these proteins are localized at ER-Golgi contact sites and two other proteins at ER-Chloroplast sites. Finally, to determine whether these proteins are involved in abiotic stress tolerance, we have analysed the root growth and seed germination rates of Arabidopsis mutants for these genes under different conditions. Some of these mutants have shown different germination rates in media supplemented with NaCl and different rates of expanded cotyledons in media supplemented with ABA. These results suggest that some these proteins may be implicated in abiotic stress signalling through an ABA-dependent pathway.es_ES
dc.description.sponsorshipUniversidad de Málaga. Campus de Excelencia Internacional Andalucía Tech. This work is supported by grants from: Ministerio de Ciencia, Innovación y Universidades (grant PGC2018-098789-B-I00), UMA-FEDER (grant UMA18-FEDERJA-154) and Ministerio de Ciencia e Innovación (BIO2017-82609-R).es_ES
dc.language.isoenges_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.subjectLípidoses_ES
dc.subjectBioquímicaes_ES
dc.subjectQuímica moleculares_ES
dc.subjectProteinases_ES
dc.subject.otherSMPes_ES
dc.subject.otherContact Siteses_ES
dc.subject.otherLipidses_ES
dc.subject.otherMembraneses_ES
dc.titleSMP-CONTAINING PROTEINS AT MEMBRANE CONTACT SITES: SUBCELLULAR LOCALIZATION AND CHARACTERIZATION.es_ES
dc.typeinfo:eu-repo/semantics/conferenceObjectes_ES
dc.centroFacultad de Cienciases_ES
dc.relation.eventtitleXXIV Meeting of the Spanish Society of Plant Biology; XVII Spanish Portuguese Congress on Plant Biologyes_ES
dc.relation.eventplaceVigo (online)es_ES
dc.relation.eventdate06/07/2021es_ES


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