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247 results on '"Díaz-Quintana, Antonio"'

1. SUMOylation controls Hu antigen R posttranscriptional activity in liver cancer

Author

Lachiondo-Ortega, Sofia, Rejano-Gordillo, Claudia M., Simon, Jorge, Lopitz-Otsoa, Fernando, C. Delgado, Teresa, Mazan-Mamczarz, Krystyna, Goikoetxea-Usandizaga, Naroa, Zapata-Pavas, L. Estefanía, García-del Río, Ana, Guerra, Pietro, Peña-Sanfélix, Patricia, Hermán-Sánchez, Natalia, Al-Abdulla, Ruba, Fernandez-Rodríguez, Carmen, Azkargorta, Mikel, Velázquez-Cruz, Alejandro, Guyon, Joris, Martín, César, Zalamea, Juan Diego, Egia-Mendikute, Leire, Sanz-Parra, Arantza, Serrano-Maciá, Marina, González-Recio, Irene, Gonzalez-Lopez, Monika, Martínez-Cruz, Luis Alfonso, Pontisso, Patrizia, Aransay, Ana M., Barrio, Rosa, Sutherland, James D., Abrescia, Nicola G.A., Elortza, Félix, Lujambio, Amaia, Banales, Jesus M., Luque, Raúl M., Gahete, Manuel D., Palazón, Asís, Avila, Matias A., G. Marin, Jose J., De, Supriyo, Daubon, Thomas, Díaz-Quintana, Antonio, Díaz-Moreno, Irene, Gorospe, Myriam, Rodríguez, Manuel S., and Martínez-Chantar, María Luz

Published
2024
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3. Neddylation of phosphoenolpyruvate carboxykinase 1 controls glucose metabolism

Author

Gonzalez-Rellan, María J., Fernández, Uxía, Parracho, Tamara, Novoa, Eva, Fondevila, Marcos F., da Silva Lima, Natalia, Ramos, Lucía, Rodríguez, Amaia, Serrano-Maciá, Marina, Perez-Mejias, Gonzalo, Chantada-Vazquez, Pilar, Riobello, Cristina, Veyrat-Durebex, Christelle, Tovar, Sulay, Coppari, Roberto, Woodhoo, Ashwin, Schwaninger, Markus, Prevot, Vincent, Delgado, Teresa C., Lopez, Miguel, Diaz-Quintana, Antonio, Dieguez, Carlos, Guallar, Diana, Frühbeck, Gema, Diaz-Moreno, Irene, Bravo, Susana B., Martinez-Chantar, Maria L., and Nogueiras, Ruben

Published
2023
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4. Nucleus-translocated mitochondrial cytochrome c liberates nucleophosmin-sequestered ARF tumor suppressor by changing nucleolar liquid–liquid phase separation

Author

González-Arzola, Katiuska, Díaz-Quintana, Antonio, Bernardo-García, Noelia, Martínez-Fábregas, Jonathan, Rivero-Rodríguez, Francisco, Casado-Combreras, Miguel Á., Elena-Real, Carlos A., Velázquez-Cruz, Alejandro, Gil-Caballero, Sergio, Velázquez-Campoy, Adrián, Szulc, Elzbieta, Gavilán, María P., Ayala, Isabel, Arranz, Rocío, Ríos, Rosa M., Salvatella, Xavier, Valpuesta, José M., Hermoso, Juan A., De la Rosa, Miguel A., and Díaz-Moreno, Irene

Published
2022
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11. SUMOylation regulates LKB1 localization and its oncogenic activity in liver cancer

Author

Zubiete-Franco, Imanol, García-Rodríguez, Juan L., Lopitz-Otsoa, Fernando, Serrano-Macia, Marina, Simon, Jorge, Fernández-Tussy, Pablo, Barbier-Torres, Lucía, Fernández-Ramos, David, Gutiérrez-de-Juan, Virginia, López de Davalillo, Sergio, Carlevaris, Onintza, Beguiristain Gómez, Adolfo, Villa, Erica, Calvisi, Diego, Martín, César, Berra, Edurne, Aspichueta, Patricia, Beraza, Naiara, Varela-Rey, Marta, Ávila, Matias, Rodríguez, Manuel S., Mato, José M., Díaz-Moreno, Irene, Díaz-Quintana, Antonio, Delgado, Teresa C., and Martínez-Chantar, María L.

Published
2019
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15. Pantothenate Rescues Iron Accumulation in Pantothenate Kinase-Associated Neurodegeneration Depending on the Type of Mutation

Author

Álvarez-Córdoba, Mónica, Fernández Khoury, Aida, Villanueva-Paz, Marina, Gómez-Navarro, Carmen, Villalón-García, Irene, Suárez-Rivero, Juan M., Povea-Cabello, Suleva, de la Mata, Mario, Cotán, David, Talaverón-Rey, Marta, Pérez-Pulido, Antonio J., Salas, Joaquín J., Pérez-Villegas, Eva Mª, Díaz-Quintana, Antonio, Armengol, José A., and Sánchez-Alcázar, José A.

Published
2019
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23. The Histone Chaperones SET/TAF-1β and NPM1 Exhibit Conserved Functionality in Nucleosome Remodeling and Histone Eviction in a Cytochrome c-Dependent Manner.

Author

Buzón, Pedro, Velázquez-Cruz, Alejandro, Corrales-Guerrero, Laura, Díaz-Quintana, Antonio, Díaz-Moreno, Irene, and Roos, Wouter H.

Subjects
NUCLEIC acid hybridization, HISTONES, EVICTION, MOLECULAR chaperones, BASE pairs, GENE expression, CONFOCAL fluorescence microscopy
Abstract

Chromatin homeostasis mediates essential processes in eukaryotes, where histone chaperones have emerged as major regulatory factors during DNA replication, repair, and transcription. The dynamic nature of these processes, however, has severely impeded their characterization at the molecular level. Here, fluorescence optical tweezers are applied to follow histone chaperone dynamics in real time. The molecular action of SET/template-activating factor-l/β and nucleophosmin 1-representing the two most common histone chaperone folds-are examined using both nucleosomes and isolated histones. It is shown that these chaperones present binding specificity for fully dismantled nucleosomes and are able to recognize and disrupt non-native histone-DNA interactions. Furthermore, the histone eviction process and its modulation by cytochrome c are scrutinized. This approach shows that despite the different structures of these chaperones, they present conserved modes of action mediating nucleosome remodeling. [ABSTRACT FROM AUTHOR]

Published
2023
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24. Mitochondrial Factors in the Cell Nucleus.

Author

González-Arzola, Katiuska and Díaz-Quintana, Antonio

Subjects
*CELL nuclei, *MITOCHONDRIA, *MITOCHONDRIAL proteins, *GENE expression, *DENATURATION of proteins, *HEAT shock proteins, *DNA damage, *HOMEOSTASIS
Abstract

The origin of eukaryotic organisms involved the integration of mitochondria into the ancestor cell, with a massive gene transfer from the original proteobacterium to the host nucleus. Thus, mitochondrial performance relies on a mosaic of nuclear gene products from a variety of genomes. The concerted regulation of their synthesis is necessary for metabolic housekeeping and stress response. This governance involves crosstalk between mitochondrial, cytoplasmic, and nuclear factors. While anterograde and retrograde regulation preserve mitochondrial homeostasis, the mitochondria can modulate a wide set of nuclear genes in response to an extensive variety of conditions, whose response mechanisms often merge. In this review, we summarise how mitochondrial metabolites and proteins—encoded either in the nucleus or in the organelle—target the cell nucleus and exert different actions modulating gene expression and the chromatin state, or even causing DNA fragmentation in response to common stress conditions, such as hypoxia, oxidative stress, unfolded protein stress, and DNA damage. [ABSTRACT FROM AUTHOR]

Published
2023
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33. GWAS of genetic factors affecting white blood cell morphological parameters in Sardinians uncovers influence of chromosome 11 innate immunity gene cluster on eosinophil morphology.

Author

Marongiu, Michele, Pérez-Mejías, Gonzalo, Orrù, Valeria, Steri, Maristella, Sidore, Carlo, Díaz-Quintana, Antonio, Mulas, Antonella, Busonero, Fabio, Maschio, Andrea, Walter, Klaudia, Tardaguila, Manuel, Akbari, Parsa, Soranzo, Nicole, Fiorillo, Edoardo, Gorospe, Myriam, Schlessinger, David, Díaz-Moreno, Irene, Cucca, Francesco, and Zoledziewska, Magdalena

Published
2023
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50. Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of Cytochrome c and Cardiolipin

Author

Díaz-Quintana, Antonio, Pérez-Mejías, Gonzalo, Guerra-Castellano, Alejandra, De la Rosa, Miguel A., and Díaz-Moreno, Irene

Subjects
Article Subject
Abstract

Cardiolipin oxidation and degradation by different factors under severe cell stress serve as a trigger for genetically encoded cell death programs. In this context, the interplay between cardiolipin and another mitochondrial factor—cytochrome c—is a key process in the early stages of apoptosis, and it is a matter of intense research. Cytochrome c interacts with lipid membranes by electrostatic interactions, hydrogen bonds, and hydrophobic effects. Experimental conditions (including pH, lipid composition, and post-translational modifications) determine which specific amino acid residues are involved in the interaction and influence the heme iron coordination state. In fact, up to four binding sites (A, C, N, and L), driven by different interactions, have been reported. Nevertheless, key aspects of the mechanism for cardiolipin oxidation by the hemeprotein are well established. First, cytochrome c acts as a pseudoperoxidase, a process orchestrated by tyrosine residues which are crucial for peroxygenase activity and sensitivity towards oxidation caused by protein self-degradation. Second, flexibility of two weakest folding units of the hemeprotein correlates with its peroxidase activity and the stability of the iron coordination sphere. Third, the diversity of the mode of interaction parallels a broad diversity in the specific reaction pathway. Thus, current knowledge has already enabled the design of novel drugs designed to successfully inhibit cardiolipin oxidation.

Published
2020
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