Katiuska Gonzalez-Arzola

@us.es

Associate Professor of Biochemistry
University of Seville / Andalusian Center of Molecular Biology and Regenerative Medicine (CABIMER)

Katiuska Gonzalez-Arzola


         Download Compact PDF  
https://researchid.co/kgonzalez
Katiuska González Arzola is Associate Professor of Biochemistry at the University of Seville, Spain. Her research work has focused in the structural features of the protein-protein interaction networks responsible for nucleolar stress signalling.

For this, she apply a broad diversity of methodologies and techniques ranging from molecular and cell biology (cloning, protein expression and purification, genetic manipulation, etc.) to biochemistry, biophysics and structural biology.

EDUCATION

She graduated in Biology in 2003 and received her PhD degree from University of La Laguna in 2010.

RESEARCH INTERESTS

Her research work has focused in the structural features of the protein-protein interaction networks responsible for nucleolar stress signalling. For this, she apply a broad diversity of methodologies and techniques ranging from molecular and cell biology (cloning, protein expression, etc).
26

Scopus Publications

Scopus Publications

  • The nucleolus: Coordinating stress response and genomic stability
    Katiuska González-Arzola
    Biochimica Et Biophysica Acta Gene Regulatory Mechanisms, 2024
  • Mitochondrial Factors in the Cell Nucleus
    Katiuska González-Arzola, Antonio Díaz-Quintana
    International Journal of Molecular Sciences, 2023
    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.
  • Nucleus-translocated mitochondrial cytochrome c liberates nucleophosmin-sequestered ARF tumor suppressor by changing nucleolar liquid–liquid phase separation
    Katiuska González-Arzola, Antonio Díaz-Quintana, Noelia Bernardo-García, Jonathan Martínez-Fábregas, Francisco Rivero-Rodríguez, Miguel Á. Casado-Combreras, Carlos A. Elena-Real, Alejandro Velázquez-Cruz, Sergio Gil-Caballero, Adrián Velázquez-Campoy, Elzbieta Szulc, María P. Gavilán, Isabel Ayala, Rocío Arranz, Rosa M. Ríos, Xavier Salvatella, José M. Valpuesta, Juan A. Hermoso, Miguel A. De la Rosa, Irene Díaz-Moreno
    Nature Structural and Molecular Biology, 2022
  • PP2A is activated by cytochrome c upon formation of a diffuse encounter complex with SET/TAF-Iβ
    Miguel Á. Casado-Combreras, Francisco Rivero-Rodríguez, Carlos A. Elena-Real, Dmitry Molodenskiy, Antonio Díaz-Quintana, Marlène Martinho, Guillaume Gerbaud, Katiuska González-Arzola, Adrián Velázquez-Campoy, Dmitri Svergun, Valérie Belle, Miguel A. De la Rosa, Irene Díaz-Moreno
    Computational and Structural Biotechnology Journal, 2022
    Intrinsic protein flexibility is of overwhelming relevance for intermolecular recognition and adaptability of highly dynamic ensemble of complexes, and the phenomenon is essential for the understanding of numerous biological processes. These conformational ensembles—encounter complexes—lack a unique organization, which prevents the determination of well-defined high resolution structures. This is the case for complexes involving the oncoprotein SET/template-activating factor-Iβ (SET/TAF-Iβ), a histone chaperone whose functions and interactions are significantly affected by its intrinsic structural plasticity. Besides its role in chromatin remodeling, SET/TAF-Iβ is an inhibitor of protein phosphatase 2A (PP2A), which is a key phosphatase counteracting transcription and signaling events controlling the activity of DNA damage response (DDR) mediators. During DDR, SET/TAF-Iβ is sequestered by cytochrome c (Cc) upon migration of the hemeprotein from mitochondria to the cell nucleus. Here, we report that the nuclear SET/TAF-Iβ:Cc polyconformational ensemble is able to activate PP2A. In particular, the N-end folded, globular region of SET/TAF-Iβ (a.k.a. SET/TAF-IβΔC)—which exhibits an unexpected, intrinsically highly dynamic behavior—is sufficient to be recognized by Cc in a diffuse encounter manner. Cc-mediated blocking of PP2A inhibition is deciphered using an integrated structural and computational approach combining small-angle X-ray scattering, electron paramagnetic resonance, nuclear magnetic resonance, calorimetry and molecular dynamics simulations.
  • Mitochondrial cytochrome c shot towards histone chaperone condensates in the nucleus
    Katiuska González‐Arzola, Alejandra Guerra‐Castellano, Francisco Rivero‐Rodríguez, Miguel Á. Casado‐Combreras, Gonzalo Pérez‐Mejías, Antonio Díaz‐Quintana, Irene Díaz‐Moreno, Miguel A. De la Rosa
    FEBS Open Bio, 2021
    Despite mitochondria being key for the control of cell homeostasis and fate, their role in DNA damage response is usually just regarded as an apoptotic trigger. However, growing evidence points to mitochondrial factors modulating nuclear functions. Remarkably, after DNA damage, cytochrome c (Cc) interacts in the cell nucleus with a variety of well‐known histone chaperones, whose activity is competitively inhibited by the haem protein. As nuclear Cc inhibits the nucleosome assembly/disassembly activity of histone chaperones, it might indeed affect chromatin dynamics and histone deposition on DNA. Several histone chaperones actually interact with Cc Lys residues through their acidic regions, which are also involved in heterotypic interactions leading to liquid–liquid phase transitions responsible for the assembly of nuclear condensates, including heterochromatin. This relies on dynamic histone–DNA interactions that can be modulated by acetylation of specific histone Lys residues. Thus, Cc may have a major regulatory role in DNA repair by fine‐tuning nucleosome assembly activity and likely nuclear condensate formation.
  • Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c
    Francisco Rivero-Rodríguez, Antonio Díaz-Quintana, Alejandro Velázquez-Cruz, Katiuska González-Arzola, Maria P. Gavilan, Adrián Velázquez-Campoy, Rosa M. Ríos, Miguel A. De la Rosa, Irene Díaz-Moreno
    Redox Biology, 2021
    Repair of injured DNA relies on nucleosome dismantling by histone chaperones and de-phosphorylation events carried out by Protein Phosphatase 2A (PP2A). Typical histone chaperones are the Acidic leucine-rich Nuclear Phosphoprotein 32 family (ANP32) members, e.g. ANP32A, which is also a well-known PP2A inhibitor (a.k.a. I1PP2A). Here we report the novel interaction between the endogenous family member B—so-called ANP32B—and endogenous cytochrome c in cells undergoing camptothecin-induced DNA damage. Soon after DNA lesions but prior to caspase cascade activation, the hemeprotein translocates to the nucleus to target the Low Complexity Acidic Region (LCAR) of ANP32B; in a similar way, our group recently reported that the hemeprotein targets the acidic domain of SET/Template Activating Factor-Iβ (SET/TAF-Iβ), which is another histone chaperone and PP2A inhibitor (a.k.a. I2PP2A). The nucleosome assembly activity of ANP32B is indeed unaffected by cytochrome c binding. Like ANP32A, ANP32B inhibits PP2A activity and is thus herein referred to as I3PP2A. Our data demonstrates that ANP32B-dependent inhibition of PP2A is regulated by respiratory cytochrome c, which induces long-distance allosteric changes in the structured N-terminal domain of ANP32B upon binding to the C-terminal LCAR. In agreement with the reported role of PP2A in the DNA damage response, we propose a model wherein cytochrome c is translocated from the mitochondria into the nucleus upon DNA damage to modulate PP2A activity via its interaction with ANP32B.
  • Proposed mechanism for regulation of H2O2-induced programmed cell death in plants by binding of cytochrome c to 14-3-3 proteins
    Carlos A. Elena‐Real, Katiuska González‐Arzola, Gonzalo Pérez‐Mejías, Antonio Díaz‐Quintana, Adrián Velázquez‐Campoy, Bénédicte Desvoyes, Crisanto Gutiérrez, Miguel A. De la Rosa, Irene Díaz‐Moreno
    Plant Journal, 2021
    Programmed cell death is crucial for development and homeostasis of all living organisms. In human cells, the double role of extra-mitochondrial cytochrome c in triggering apoptosis and inhibiting survival pathways is well reported. In plants, however, the specific role of cytochrome c upon release from the mitochondria remains in part veiled yet death stimuli do trigger cytochrome c translocation as well. Here, we identify an Arabidopsis thaliana 14-3-3ι isoform as a cytosolic cytochrome c target and inhibitor of caspase-like activity. This finding establishes the 14-3-3ι protein as a relevant factor at the onset of plant H2 O2 -induced programmed cell death. The in vivo and in vitro studies herein reported reveal that the interaction between cytochrome c and 14-3-3ι exhibits noticeable similarities with the complex formed by their human orthologues. Further analysis of the heterologous complexes between human and plant cytochrome c with plant 14-3-3ι and human 14-3-3ε isoforms corroborated common features. These results suggest that cytochrome c blocks p14-3-3ι so as to inhibit caspase-like proteases, which in turn promote cell death upon H2 O2 -treatment. Besides establishing common biochemical features between human and plant programmed cell death, this work sheds light onto the signaling networks of plant cell death.
  • Exploring protein phosphorylation by combining computational approaches and biochemical methods
    Gonzalo Pérez-Mejías, Alejandro Velázquez-Cruz, Alejandra Guerra-Castellano, Blanca Baños-Jaime, Antonio Díaz-Quintana, Katiuska González-Arzola, Miguel Ángel De la Rosa, Irene Díaz-Moreno
    Computational and Structural Biotechnology Journal, 2020
    Post-translational modifications of proteins expand their functional diversity, regulating the response of cells to a variety of stimuli. Among these modifications, phosphorylation is the most ubiquitous and plays a prominent role in cell signaling. The addition of a phosphate often affects the function of a protein by altering its structure and dynamics. However, these alterations are often difficult to study and the functional and structural implications remain unresolved. New approaches are emerging to overcome common obstacles related to the production and manipulation of these samples. Here, we summarize the available methods for phosphoprotein purification and phosphomimetic engineering, highlighting the advantages and disadvantages of each. We propose a general workflow for protein phosphorylation analysis combining computational and biochemical approaches, building on recent advances that enable user-friendly and easy-to-access Molecular Dynamics simulations. We hope this innovative workflow will inform the best experimental approach to explore such post-translational modifications. We have applied this workflow to two different human protein models: the hemeprotein cytochrome c and the RNA binding protein HuR. Our results illustrate the usefulness of Molecular Dynamics as a decision-making tool to design the most appropriate phosphomimetic variant.
  • New moonlighting functions of mitochondrial cytochrome c in the cytoplasm and nucleus
    Katiuska González‐Arzola, Alejandro Velázquez‐Cruz, Alejandra Guerra‐Castellano, Miguel Á. Casado‐Combreras, Gonzalo Pérez‐Mejías, Antonio Díaz‐Quintana, Irene Díaz‐Moreno, Miguel Á. De la Rosa
    FEBS Letters, 2019
    Cytochrome c (Cc) is a protein that functions as an electron carrier in the mitochondrial respiratory chain. However, Cc has moonlighting roles outside mitochondria driving the transition of apoptotic cells from life to death. When living cells are damaged, Cc escapes its natural mitochondrial environment and, once in the cytosol, it binds other proteins to form a complex named the apoptosome—a platform that triggers caspase activation and further leads to controlled cell dismantlement. Early released Cc also binds to inositol 1,4,5‐triphosphate receptors on the ER membrane, which stimulates further massive Cc release from mitochondria. Besides the well‐characterized binding proteins contributing to the proapoptotic functions of Cc, many novel protein targets have been recently described. Among them, histone chaperones were identified as key partners of Cc following DNA breaks, indicating that Cc might modulate chromatin dynamics through competitive binding to histone chaperones. In this article, we review the ample set of recently discovered antiapoptotic proteins—involved in DNA damage, transcription, and energetic metabolism—reported to interact with Cc in the cytoplasm and even the nucleus upon DNA breaks.
  • Oxidative stress is tightly regulated by cytochrome c phosphorylation and respirasome factors in mitochondria
    Alejandra Guerra-Castellano, Antonio Díaz-Quintana, Gonzalo Pérez-Mejías, Carlos A. Elena-Real, Katiuska González-Arzola, Sofía M. García-Mauriño, Miguel A. De la Rosa, Irene Díaz-Moreno
    Proceedings of the National Academy of Sciences of the United States of America, 2018
    Significance Dysfunction of mitochondria, the powerhouses of living cells, favors the onset of human diseases, namely neurodegenerative diseases, cardiovascular pathologies, and cancer. Actually, respiratory cytochrome c has been found to be phosphorylated at tyrosine 97 during the insulin-induced neuroprotection response following a brain ischemic injury. Here, we report that the decrease in neuronal death could be directly ascribed to changes in mitochondrial metabolism—including lower production of reactive oxygen species—and cell homeostasis induced by cytochrome c phosphorylation. Our findings thus provide the basis for understanding the molecular mechanism and potential use of phosphomimetic species of cytochrome c , thereby yielding new opportunities to develop more efficient therapies against acute pathologies.
  • Cytochrome c speeds up caspase cascade activation by blocking 14-3-3ϵ-dependent Apaf-1 inhibition article
    Carlos A. Elena-Real, Antonio Díaz-Quintana, Katiuska González-Arzola, Adrián Velázquez-Campoy, Mar Orzáez, Abelardo López-Rivas, Sergio Gil-Caballero, Miguel Á. De la Rosa, Irene Díaz-Moreno
    Cell Death and Disease, 2018
  • Structural basis of mitochondrial dysfunction in response to cytochrome c phosphorylation at tyrosine 48
    Blas Moreno-Beltrán, Alejandra Guerra-Castellano, Antonio Díaz-Quintana, Rebecca Del Conte, Sofía M. García-Mauriño, Sofía Díaz-Moreno, Katiuska González-Arzola, Carlos Santos-Ocaña, Adrián Velázquez-Campoy, Miguel A. De la Rosa, Paola Turano, Irene Díaz-Moreno
    Proceedings of the National Academy of Sciences of the United States of America, 2017
  • Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome c
    Katiuska González-Arzola, Antonio Díaz-Quintana, Francisco Rivero-Rodríguez, Adrián Velázquez-Campoy, Miguel A. De la Rosa, Irene Díaz-Moreno
    Nucleic Acids Research, 2017
  • Cytochrome c–Based Signalosome
    BLAS MORENO-BELTRÁN KATIUSKA GONZÁLEZ-ARZOLA
    Redox Proteins in Supercomplexes and Signalosomes, 2016
  • Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c
    Katiuska González-Arzola, Irene Díaz-Moreno, Ana Cano-González, Antonio Díaz-Quintana, Adrián Velázquez-Campoy, Blas Moreno-Beltrán, Abelardo López-Rivas, Miguel A. De la Rosa
    Proceedings of the National Academy of Sciences of the United States of America, 2015
  • Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength
    Blas Moreno-Beltrán, Irene Díaz-Moreno, Katiuska González-Arzola, Alejandra Guerra-Castellano, Adrián Velázquez-Campoy, Miguel A. De la Rosa, Antonio Díaz-Quintana
    FEBS Letters, 2015
  • A common signalosome for programmed cell death in humans and plants
    J Martínez-Fábregas, I Díaz-Moreno, K González-Arzola, A Díaz-Quintana, M A De la Rosa
    Cell Death and Disease, 2014
  • Cytochrome c1 exhibits two binding sites for cytochrome c in plants
    Blas Moreno-Beltrán, Antonio Díaz-Quintana, Katiuska González-Arzola, Adrián Velázquez-Campoy, Miguel A. De la Rosa, Irene Díaz-Moreno
    Biochimica Et Biophysica Acta Bioenergetics, 2014
  • Structural and functional analysis of novel human cytochrome c targets in apoptosis
    Jonathan Martínez-Fábregas, Irene Díaz-Moreno, Katiuska González-Arzola, Simon Janocha, José A. Navarro, Manuel Hervás, Rita Bernhardt, Adrián Velázquez-Campoy, Antonio Díaz-Quintana, Miguel A. De la Rosa
    Molecular and Cellular Proteomics, 2014
  • New arabidopsis thaliana cytochrome c partners: A look into the elusive role of cytochrome c in programmed cell death inplants
    Jonathan Martínez-Fábregas, Irene Díaz-Moreno, Katiuska González-Arzola, Simon Janocha, José A. Navarro, Manuel Hervás, Rita Bernhardt, Antonio Díaz-Quintana, Miguel Á. De la Rosa
    Molecular and Cellular Proteomics, 2013
  • Recent methodological advances in the analysis of protein tyrosine nitration
    Irene Díaz-Moreno, José M. García-Heredia, Katiuska González-Arzola, Antonio Díaz-Quintana, Miguel Á. De la Rosa
    Chemphyschem, 2013
  • Adsorption of a laccase from fusarium proliferatum on Au(111) and HOPG electrodes: A scanning probe microscopy and electrochemical approach
    International Journal of Electrochemical Science, 2012
  • Electrochemical and AFM characterization on gold and carbon electrodes of a high redox potential laccase from Fusarium proliferatum
    K. González Arzola, Y. Gimeno, M.C. Arévalo, M.A. Falcón, A. Hernández Creus
    Bioelectrochemistry, 2010
  • Catalytic efficiency of natural and synthetic compounds used as laccase-mediators in oxidising veratryl alcohol and a kraft lignin, estimated by electrochemical analysis
    K. González Arzola, M.C. Arévalo, M.A. Falcón
    Electrochimica Acta, 2009
  • Early attack and subsequent changes produced in an industrial lignin by a fungal laccase and a laccase-mediator system: An analytical approach
    K. González Arzola, O. Polvillo, M. E. Arias, F. Perestelo, A. Carnicero, F. J. González-Vila, M. A. Falcón
    Applied Microbiology and Biotechnology, 2006
  • Production, partial characterization and mass spectrometric studies of the extracellular laccase activity from Fusarium proliferatum
    J.R. Hernández Fernaud, A. Marina, K. González, J. Vázquez, M. A. Falcón
    Applied Microbiology and Biotechnology, 2006