11 results on '"González‐Arzola, Katiuska"'
Search Results
2. Nucleus-translocated mitochondrial cytochrome c liberates nucleophosmin-sequestered ARF tumor suppressor by changing nucleolar liquid–liquid phase separation
- Author
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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
- Full Text
- View/download PDF
3. PP2A is activated by cytochrome c upon formation of a diffuse encounter complex with SET/TAF-Iβ
- Author
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Casado-Combreras, Miguel Á., Rivero-Rodríguez, Francisco, Elena-Real, Carlos A., Molodenskiy, Dmitry, Díaz-Quintana, Antonio, Martinho, Marlène, Gerbaud, Guillaume, González-Arzola, Katiuska, Velázquez-Campoy, Adrián, Svergun, Dmitri, Belle, Valérie, De la Rosa, Miguel A., and Díaz-Moreno, Irene
- Published
- 2022
- Full Text
- View/download PDF
4. Mitochondrial Factors in the Cell Nucleus
- Author
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Junta de Andalucía, González-Arzola, Katiuska [0000-0002-1124-3847], Díaz-Quintana, Antonio [0000-0001-8973-8009], González-Arzola, Katiuska, Díaz-Quintana, Antonio, Junta de Andalucía, González-Arzola, Katiuska [0000-0002-1124-3847], Díaz-Quintana, Antonio [0000-0001-8973-8009], González-Arzola, Katiuska, and Díaz-Quintana, Antonio
- 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.
- Published
- 2023
5. Metabolismo de azúcares tras la ingesta de alimentos
- Author
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González García, María de la Cruz, primary, Huertas Romera, María José, additional, González Arzola, Katiuska, additional, Aroca Aguilar, Ángeles, additional, Molina Heredia, Fernando Publio, additional, Naranjo Río-Miranda, Belén, additional, Ojeda Servián, Valle, additional, and Casatejada Pérez, María Azahara, additional
- Published
- 2023
- Full Text
- View/download PDF
6. Mitochondrial Factors in the Cell Nucleus
- Author
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González-Arzola, Katiuska, primary and Díaz-Quintana, Antonio, additional
- Published
- 2023
- Full Text
- View/download PDF
7. Nucleus-translocated mitochondrial cytochrome c liberates nucleophosmin-sequestered ARF tumor suppressor by changing nucleolar liquid-liquid phase separation
- Author
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Universidad de Sevilla, ALBA Synchrotron, Ministerio de Economía y Competitividad (España), Ministerio de Ciencia e Innovación (España), Junta de Andalucía, European Commission, Fundación Ramón Areces, Ministerio de Educación, Cultura y Deporte (España), Fundación la Caixa, Fundación Científica Asociación Española Contra el Cáncer, González-Arzola, Katiuska [0000-0002-1124-3847], Díaz-Quintana, Antonio [0000-0001-8973-8009], Martínez-Fábregas, Jonathan [0000-0001-5809-065X], Casado-Combreras, Miguel Á. [0000-0003-3375-7758], Velázquez-Cruz, Alejandro [0000-0002-4589-0989], Velázquez-Campoy, Adrián [0000-0001-5702-4538], Gavilán, María P. [0000-0003-3694-8525], Arranz, Rocío [0000-0001-5321-0915], Salvatella, Xavier [0000-0002-8371-4185], Valpuesta, José M. [0000-0001-7468-8053], Hermoso, Juan A. [0000-0002-1862-8950], Rosa, Miguel A. de la [0000-0003-1187-5737], Díaz-Moreno, Irene [0000-0002-5318-7644], 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., Rosa, Miguel A. de la, Díaz-Moreno, Irene, Universidad de Sevilla, ALBA Synchrotron, Ministerio de Economía y Competitividad (España), Ministerio de Ciencia e Innovación (España), Junta de Andalucía, European Commission, Fundación Ramón Areces, Ministerio de Educación, Cultura y Deporte (España), Fundación la Caixa, Fundación Científica Asociación Española Contra el Cáncer, González-Arzola, Katiuska [0000-0002-1124-3847], Díaz-Quintana, Antonio [0000-0001-8973-8009], Martínez-Fábregas, Jonathan [0000-0001-5809-065X], Casado-Combreras, Miguel Á. [0000-0003-3375-7758], Velázquez-Cruz, Alejandro [0000-0002-4589-0989], Velázquez-Campoy, Adrián [0000-0001-5702-4538], Gavilán, María P. [0000-0003-3694-8525], Arranz, Rocío [0000-0001-5321-0915], Salvatella, Xavier [0000-0002-8371-4185], Valpuesta, José M. [0000-0001-7468-8053], Hermoso, Juan A. [0000-0002-1862-8950], Rosa, Miguel A. de la [0000-0003-1187-5737], Díaz-Moreno, Irene [0000-0002-5318-7644], 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., Rosa, Miguel A. de la, and Díaz-Moreno, Irene
- Abstract
The regular functioning of the nucleolus and nucleus-mitochondria crosstalk are considered unrelated processes, yet cytochrome c (Cc) migrates to the nucleus and even the nucleolus under stress conditions. Nucleolar liquid-liquid phase separation usually serves the cell as a fast, smart mechanism to control the spatial localization and trafficking of nuclear proteins. Actually, the alternative reading frame (ARF), a tumor suppressor protein sequestered by nucleophosmin (NPM) in the nucleoli, is shifted out from NPM upon DNA damage. DNA damage also triggers early translocation of respiratory Cc to nucleus before cytoplasmic caspase activation. Here, we show that Cc can bind to nucleolar NPM by triggering an extended-to-compact conformational change, driving ARF release. Such a NPM-Cc nucleolar interaction can be extended to a general mechanism for DNA damage in which the lysine-rich regions of Cc-rather than the canonical, arginine-rich stretches of membrane-less organelle components-controls the trafficking and availability of nucleolar proteins.
- Published
- 2022
8. Papel del citocromo c en la respiración celular y regulación por modificaciones postraduccionales.
- Author
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González Arzola, Katiuska, Universidad de Sevilla. Bioquímica Vegetal y Biología Molecular., Conejero Guillén, Andrés, González Arzola, Katiuska, Universidad de Sevilla. Bioquímica Vegetal y Biología Molecular., and Conejero Guillén, Andrés
- Abstract
El citocromo c es una proteína pequeña y globular cuya función principal consiste en actuar como un transportador electrónico móvil entre los complejos III y IV de la cadena de transporte de electrones mitocondrial. Asimismo, se encuentra aparentemente implicado en la estabilidad estructural de los complejos mitocondriales I, III y IV y posiblemente también en la estabilidad estructural de los supercomplejos mitocondriales. El citocromo c se considera actualmente una proteína multifuncional de clave importancia para la homeostasis celular, que, además de sus funciones en la fosforilación oxidativa, se encuentra implicada en procesos como la apoptosis y potencialmente en la respuesta al daño en el DNA. El presente trabajo analizará el papel del citocromo c en el metabolismo energético y cómo el mismo se regula mediante diferentes modificaciones postraduccionales, las cuales alteran la funcionalidad de la proteína. Asimismo, se describirán los mecanismos de transferencia electrónica del citocromo c.
- Published
- 2023
9. Mitochondrial Factors in the Cell Nucleus
- Author
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Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular, Junta de Andalucía, González Arzola, Katiuska, Díaz Quintana, Antonio Jesús, Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular, Junta de Andalucía, González Arzola, Katiuska, and Díaz Quintana, Antonio Jesús
- 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.
- Published
- 2023
10. Nucleus-translocated mitochondrial cytochrome c liberates nucleophosmin-sequestered ARF tumor suppressor by changing nucleolar liquid-liquid phase separation.
- Author
-
Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular, Gobierno de España, Ministerio de Ciencia e Innovación (MICIN). España, Agencia Estatal de Investigación. España, European Commission (EC). Fondo Europeo de Desarrollo Regional (FEDER), Junta de Andalucía, González Arzola, Katiuska, Díaz Quintana, Antonio Jesús, Bernardo García, Noelia, Martínez Fábregas, Jonathan, Rivero Rodríguez, Francisco, Casado Combreras, Miguel Ángel, Elena-Real, Carlos A., Velázquez Cruz, Alejandro, Gil Caballero, Sergio, Velázquez Campoy, Adrián, Szulc, Elzbieta, Gavilán Dorronzoro, María de la Paz, Ayala, Isabel, Arranz, Rocío, Ríos, Rosa M., Salvatella, Xavier, Valpuesta, José María, Hermoso, Juan A., Rosa Acosta, Miguel Ángel de la, Díaz Moreno, Irene, Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular, Gobierno de España, Ministerio de Ciencia e Innovación (MICIN). España, Agencia Estatal de Investigación. España, European Commission (EC). Fondo Europeo de Desarrollo Regional (FEDER), Junta de Andalucía, González Arzola, Katiuska, Díaz Quintana, Antonio Jesús, Bernardo García, Noelia, Martínez Fábregas, Jonathan, Rivero Rodríguez, Francisco, Casado Combreras, Miguel Ángel, Elena-Real, Carlos A., Velázquez Cruz, Alejandro, Gil Caballero, Sergio, Velázquez Campoy, Adrián, Szulc, Elzbieta, Gavilán Dorronzoro, María de la Paz, Ayala, Isabel, Arranz, Rocío, Ríos, Rosa M., Salvatella, Xavier, Valpuesta, José María, Hermoso, Juan A., Rosa Acosta, Miguel Ángel de la, and Díaz Moreno, Irene
- Abstract
The regular functioning of the nucleolus and nucleus-mitochondria crosstalk are considered unrelated processes, yet cytochrome c (Cc) migrates to the nucleus and even the nucleolus under stress conditions. Nucleolar liquid–liquid phase separation usually serves the cell as a fast, smart mechanism to control the spatial localization and trafcking of nuclear proteins. Actually, the alternative reading frame (ARF), a tumor suppressor protein sequestered by nucleophosmin (NPM) in the nucleoli, is shifted out from NPM upon DNA damage. DNA damage also triggers early translocation of respiratory Cc to nucleus before cytoplasmic caspase activation. Here, we show that Cc can bind to nucleolar NPM by triggering an extended-to-compact conformational change, driving ARF release. Such a NPM–Cc nucleolar interaction can be extended to a general mechanism for DNA damage in which the lysine-rich regions of Cc—rather than the canonical, arginine-rich stretches of membrane-less organelle components—controls the trafcking and availability of nucleolar proteins.
- Published
- 2022
11. Nucleus-translocated mitochondrial cytochrome cliberates 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
- Abstract
The regular functioning of the nucleolus and nucleus-mitochondria crosstalk are considered unrelated processes, yet cytochrome c(Cc) migrates to the nucleus and even the nucleolus under stress conditions. Nucleolar liquid–liquid phase separation usually serves the cell as a fast, smart mechanism to control the spatial localization and trafficking of nuclear proteins. Actually, the alternative reading frame (ARF), a tumor suppressor protein sequestered by nucleophosmin (NPM) in the nucleoli, is shifted out from NPM upon DNA damage. DNA damage also triggers early translocation of respiratory Ccto nucleus before cytoplasmic caspase activation. Here, we show that Cccan bind to nucleolar NPM by triggering an extended-to-compact conformational change, driving ARF release. Such a NPM–Ccnucleolar interaction can be extended to a general mechanism for DNA damage in which the lysine-rich regions of Cc—rather than the canonical, arginine-rich stretches of membrane-less organelle components—controls the trafficking and availability of nucleolar proteins.
- Published
- 2022
- Full Text
- View/download PDF
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