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    Listar por autor "Morello-López, Jorge"

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      • Analysis of Arabidopsis SYT1 mutants and chimeras reveal insights about its dynamic and function on ER-PM MCS. 

        Morello-López, Jorge; Benítez-Fuente, Francisco; Collado, Javier; Fernández-Busnadiego, Rubén; Ruiz-López, NoemíAutoridad Universidad de Málaga; Botella-Mesa, Miguel ÁngelAutoridad Universidad de Málaga[et al.] (2023)
        The endoplasmic reticulum (ER) extends throughout the cell and forms Membrane Contact Sites (MCS) with other organelles. MCS are essential for lipid transport, calcium signaling and organelle communication. In plants, ...
      • Characterization of the ripe fruit epidermis-specific FvMYB29-FvbHLH transcription factors complexes in woodland strawberry. 

        Perotti, Maria Florencia; Sánchez-Gómez, Carlos; Meco, Victoriano; Morello-López, Jorge; Ruiz-López, NoemíAutoridad Universidad de Málaga; Zeisler, Viktoria Valeska; Schreiber, Lukas; Bayer, Emmanuelle M.; Franco-Zorrilla, José M.; Martín-Pizarro, Carmen; Posé-Padilla, DavidAutoridad Universidad de Málaga[et al.] (2024)
        Three out of the several ripe epidermis-specific TFs were selected to study their biological role, one of them belonging to the MYB family (FvMYB29), and two bHLH-like proteins (FvbHLH22 and FvbHLH67). Protein interaction ...
      • Characterizing SYT6, a lipid transfer protein at the secretory pathway. 

        Moya-Barrientos, Miriam; Huércano, Carolina; Morello-López, Jorge; Cardeñas Echevarría, Carlos; Boutté, Yohann; Sánchez-Vera, Victoria; Ruiz-López, NoemíAutoridad Universidad de Málaga[et al.] (2024)
        The SYT6 protein from A. thaliana 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 ...
      • Identification of NTMC2T5, a new lipid transfer protein family at ER-chloroplast contact sites involved in stress response 

        Huércano Rubens, Carolina; Percio-Vargas, Francisco; Sánchez-Vera, Victoria; Morello-López, Jorge; Salas-Liñán, Joaquín J; Ruiz-López, NoemíAutoridad Universidad de Málaga[et al.] (2022-09)
        Plants are sessile organisms and they have perfected a complex molecular signalling network to detect and respond to different environmental stresses. In plants, fatty acid synthesis takes place at chloroplasts, and they ...
      • Localization and characterization of SMP-containing proteins in Membrane Contact Sites 

        Huércano Rubens, Carolina; Sánchez-Vera, Victoria; Percio-Vargas, Francisco; Morello-López, Jorge; Botella-Mesa, Miguel ÁngelAutoridad Universidad de Málaga; Ruiz-López, NoemíAutoridad Universidad de Málaga[et al.] (2021)
        Membrane contact sites (MCS) are discrete regions where two membranes from different organelles are closely apposed (10-30 nm). In those regions, non-vesicular transfer of lipids takes place to ensure proper organelle ...
      • NTMC2T5 protein family: newly identified ER-chloroplast contact site proteins involved in abiotic stress. 

        Morello-López, Jorge; Salas-Liñán, Joaquín J; Ruiz-López, NoemíAutoridad Universidad de Málaga; Huércano Rubens, Carolina (2022-08)
        Plants are sessile organisms and therefore they have perfected a complex molecular signalling network to detect and respond to the different environmental stresses such as high temperatures, salinity, or drought. In plants, ...
      • NTMC2T5: lipid transfer proteins at ER-chloroplast contact sites involved in plant stress. 

        Huércano Rubens, Carolina; Morello-López, Jorge; Salas-Liñán, Joaquín J; Ruiz-López, NoemíAutoridad Universidad de Málaga (2022-09)
        Chloroplasts are the site of fatty acid synthesis in plants; however, these fatty acids are assembled into glycerolipids at the ER. Later on, some of these ER-assembled glycerolipids will be transferred back to the ...
      • NTMC2T5: newly identified lipid transfer proteins at ER-chloroplast contact sites. 

        Salas-Liñán, Joaquín J; Cuevas Corral, Oliver; Morello-López, Jorge; Ruiz-López, NoemíAutoridad Universidad de Málaga; Huércano Rubens, Carolina (2022)
        In plants, fatty acid synthesis takes place at chloroplasts, and they are assembled into glycerolipids and sphingolipids at the endoplasmic reticulum (ER). Then, the newly synthetized lipids in the ER are delivered to ...
      • SMP-containing proteins at membrane contact sites: subcellular localization and characterization. 

        Huércano Rubens, Carolina; Percio-Vargas, Francisco; Sánchez-Vera, Victoria; Morello-López, Jorge; Botella-Mesa, Miguel ÁngelAutoridad Universidad de Málaga; Ruiz-López, NoemíAutoridad Universidad de Málaga[et al.] (2021)
        Membrane 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 ...
      • SYT6 protein role in Arabidopsis thaliana contact sites. 

        Moya-Barrientos, Miriam; Huércano Rubens, Carolina; Morello-López, Jorge; Cardeñas Echevarría, Carlos; Boutté, Yohann; Sánchez-Vera, Victoria; Ruiz-López, NoemíAutoridad Universidad de Málaga[et al.] (2024)
        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 ...
      • SYT6: a newly identified protein involved in ER - trans-Golgi network Membrane Contact Sites 

        Morello-López, Jorge; Huércano Rubens, Carolina; Albert, Armando; Ruiz-López, NoemíAutoridad Universidad de Málaga (2022)
        SYT6 is a newly identified lipid transport protein from ER - trans-Golgi network Membrane Contact Sites. Our results show that: • SYT6 contacts trans-Golgi network vesicles through its coiled-coil domain. • SYT6 can ...
        REPOSITORIO INSTITUCIONAL UNIVERSIDAD DE MÁLAGA
        REPOSITORIO INSTITUCIONAL UNIVERSIDAD DE MÁLAGA
         

         

        REPOSITORIO INSTITUCIONAL UNIVERSIDAD DE MÁLAGA
        REPOSITORIO INSTITUCIONAL UNIVERSIDAD DE MÁLAGA