Corbalán García,  Senena

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Corbalán García, Senena

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Corbalán García, Senena

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Universidad de Murcia. Departamento de Bioquímica y Biología MolecularA

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Open Access
PKCε controls the fusion of secretory vesicles in mast cells in a phosphatidic acid-dependent mode
(ELSEVIER, 2021-06-18) Serrano-Lopez, Emilio M.; Lopez-Martínez, David; Gomez-Fernandez, Juan C.; Corbalán García, Senena; Bioquímica y Biología Molecular A
PKCε is highly expressed in mast cells and plays a fundamental role in the antigen-triggered activation of the allergic reaction. Although its regulation by diacylglycerols has been described, its regulation by acidic phospholipids and how this regulation leads to the control of downstream vesicle secretion is barely known. Here, we used structural and evolutionary studies to find the molecular mechanism that explains the selectivity of the C1B domain of PKCε by Phosphatidic Acid (PA). This resided in a collection of Arg residues that form a specific rim on the outer surface of the C1B domain, around the diacylglycerol binding cleft. In RBL-2H3 cells, this basic rim allowed the kinase to respond specifically to phosphatidic acid signals that induced its translocation to the plasma membrane and subsequent activation. Further experiments in cells that overexpress PKCε and a mutant of the PA binding site, showed that PA-dependent PKCε activation increased vesicle degranulation in RBL-2H3 cells, and this correlated with increased SNAP23 phosphorylation. Over-expression of PKCε in these cells also induced an increase in the number of docked vesicles containing SNAP23, when stimulated with PA. This accumulation could be attributed to the stabilizing effect of phosphorylation on the formation of the SNARE complex, which ultimately led to increased release of content in the presence of Ca2+ during the fusion process. Therefore, these findings reinforce the importance of PA signaling in the activation of PKCε, which could be an important target to inhibit the exacerbated responses of these cells in the allergic reaction.
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Both idebenone and idebenol are localized near the lipid-water interface of the membrane and increase its fluidity.
(2016-06-01) Torrecillas, Alejandro; de Godos, Ana M; Gómez-Fernández, Juan C; Gómez Murcia, Victoria; Corbalán García, Senena; Bioquímica y Biología Molecular A
Idebenone is a synthetic analog of coenzyme Q; both share a quinone moiety but idebenone has a shorter lipophilic tail ending with a hydroxyl group. Differential scanning calorimetry experiments showed that both idebenone and idebenol widened and shifted the phase transition of 1,2-dipalmitoylphosphatidylcholine (DPPC) to a lower temperature and a phase separation with different concentrations of these molecules was observed. Also small angle X-ray diffraction and wide angle X-ray diffraction revealed that both, idebenone and idebenol, induced laterally separated phases in fluid membranes when included in DPPC membranes. Electronic profiles showed that both forms, idebenone and idebenol, reduced the thickness of the fluid membrane. (2)H NMR measurements showed that the order of the membrane decreased at all temperatures in the presence of idebenone or idebenol, the greatest disorder being observed in the segments of the acyl chains close to the lipid-water interface. (1)H NOESY MAS NMR spectra were obtained using 1-palmitoyl-2-oleoyl-phosphatidylcholine membranes and results pointed to a similar location in the membrane for both forms, with the benzoquinone or benzoquinol rings and their terminal hydroxyl group of the hydrophobic chain located near the lipid/water interface of the phospholipid bilayer and the terminal hydroxyl group of the hydrophobic chain of both compounds located at the lipid/water interface. Taken together, all these different locations might explain the different physiological behavior shown by the idebenone/idebenol compared with the ubiquinone-10/ubiquinol-10 pair in which both compounds are differently localized in the membrane.
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Contribución al estudio de la estructura y función de la Ca2+-ATPasa del retículo sarcoplásmico / María Senena Corbalán García ; directores Juan Carmelo Gómez Fernández, José Antonio Teruel Puche.
(Murcia : Universidad de Murcia, Facultad de Veterinaria, Departamento de Bioquímica y Biología Molecular (A),, 1994) Corbalán García, Senena
Open Access
Señalización celular: PKC y cáncer
(Universidad de Murcia. Facultad de Biología, 2013) Coronado-Parra, Maria Teresa; Corbalán García, Senena
Open Access
Mecanismo de Doble Diana de las Proteínas Periféricas de Membrana
(Universidad de Murcia, 2018) Coronado-Parra, Maria Teresa; Corbalán García, Senena
Gran cantidad de funciones celulares dependen de la interacción de proteínas con la superficie interna de la membrana plasmática o de otras membranas intracelulares. Entre otras funciones destacan el tráfico celular, las rutas de señalización y el mantenimiento de la propia estructura celular. (Lemmon, 2008; Moravcevic, Oxley, & Lemmon, 2012). Entre un 30-40% de las proteínas celulares existentes interaccionan con algún tipo de membrana, manifestando así la importancia de las funciones que desempeñan (Arora & Tamm, 2001).