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  1. AU="Domínguez-Zorita, Sonia"
  2. AU="Nakashima, Ayaka"
  3. AU="Skorecki, Karl"
  4. AU=Ibrahim Salwa
  5. AU=Geocadin Romergryko G
  6. AU="Leroy, J"
  7. AU="Wilson, Peter H"
  8. AU="Cunha, Carla Baroni"

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  1. Article: The ATPase Inhibitory Factor 1 (IF1) Contributes to the Warburg Effect and Is Regulated by Its Phosphorylation in S39 by a Protein Kinase A-like Activity.

    Cuezva, José M / Domínguez-Zorita, Sonia

    Cancers

    2024  Volume 16, Issue 5

    Abstract: The relevant role played by the ATPase Inhibitory Factor 1 (IF1) as a physiological in vivo inhibitor of mitochondrial ATP synthase in cancer and non-cancer cells, and in the mitochondria of different mouse tissues, as assessed in different genetic loss- ...

    Abstract The relevant role played by the ATPase Inhibitory Factor 1 (IF1) as a physiological in vivo inhibitor of mitochondrial ATP synthase in cancer and non-cancer cells, and in the mitochondria of different mouse tissues, as assessed in different genetic loss- and gain-of-function models of IF1 has been extensively documented. In this review we summarize our findings and those of others that favor the implication of IF1 in metabolic reprogramming to an enhanced glycolytic phenotype, which is mediated by its binding and inhibition of the ATP synthase. Moreover, we emphasize that IF1 is phosphorylated in vivo in its S39 by the c-AMP-dependent PKA activity of mitochondria to render an inactive inhibitor that is unable to interact with the enzyme, thus triggering the activation of ATP synthase. Overall, we discuss and challenge the results that argue against the role of IF1 as in vivo inhibitor of mitochondrial ATP synthase and stress that IF1 cannot be regarded solely as a pro-oncogenic protein because in some prevalent carcinomas, it prevents metastatic disease.
    Language English
    Publishing date 2024-02-29
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2527080-1
    ISSN 2072-6694
    ISSN 2072-6694
    DOI 10.3390/cancers16051014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: The Mitochondrial ATP Synthase/IF1 Axis in Cancer Progression: Targets for Therapeutic Intervention.

    Domínguez-Zorita, Sonia / Cuezva, José M

    Cancers

    2023  Volume 15, Issue 15

    Abstract: Cancer poses a significant global health problem with profound personal and economic implications on National Health Care Systems. The reprograming of metabolism is a major trait of the cancer phenotype with a clear potential for developing effective ... ...

    Abstract Cancer poses a significant global health problem with profound personal and economic implications on National Health Care Systems. The reprograming of metabolism is a major trait of the cancer phenotype with a clear potential for developing effective therapeutic strategies to combat the disease. Herein, we summarize the relevant role that the mitochondrial ATP synthase and its physiological inhibitor, ATPase Inhibitory Factor 1 (IF1), play in metabolic reprogramming to an enhanced glycolytic phenotype. We stress that the interplay in the ATP synthase/IF1 axis has additional functional roles in signaling mitohormetic programs, pro-oncogenic or anti-metastatic phenotypes depending on the cell type. Moreover, the same axis also participates in cell death resistance of cancer cells by restrained mitochondrial permeability transition pore opening. We emphasize the relevance of the different post-transcriptional mechanisms that regulate the specific expression and activity of ATP synthase/IF1, to stimulate further investigations in the field because of their potential as future targets to treat cancer. In addition, we review recent findings stressing that mitochondria metabolism is the primary altered target in lung adenocarcinomas and that the ATP synthase/IF1 axis of OXPHOS is included in the most significant signature of metastatic disease. Finally, we stress that targeting mitochondrial OXPHOS in pre-clinical mouse models affords a most effective therapeutic strategy in cancer treatment.
    Language English
    Publishing date 2023-07-25
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2527080-1
    ISSN 2072-6694
    ISSN 2072-6694
    DOI 10.3390/cancers15153775
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: The ATPase Inhibitory Factor 1 is a Tissue-Specific Physiological Regulator of the Structure and Function of Mitochondrial ATP Synthase: A Closer Look Into Neuronal Function.

    Domínguez-Zorita, Sonia / Romero-Carramiñana, Inés / Cuezva, José M / Esparza-Moltó, Pau B

    Frontiers in physiology

    2022  Volume 13, Page(s) 868820

    Abstract: The ATP synthase is an essential multifunctional enzyme complex of mitochondria that produces most of cellular ATP, shapes the structure of the inner membrane into cristae and regulates the signals that control cell fate or demise. The ATPase Inhibitory ... ...

    Abstract The ATP synthase is an essential multifunctional enzyme complex of mitochondria that produces most of cellular ATP, shapes the structure of the inner membrane into cristae and regulates the signals that control cell fate or demise. The ATPase Inhibitory Factor 1 (IF1) functions
    Language English
    Publishing date 2022-03-18
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2022.868820
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: IF1 promotes oligomeric assemblies of sluggish ATP synthase and outlines the heterogeneity of the mitochondrial membrane potential.

    Romero-Carramiñana, Inés / Esparza-Moltó, Pau B / Domínguez-Zorita, Sonia / Nuevo-Tapioles, Cristina / Cuezva, José M

    Communications biology

    2023  Volume 6, Issue 1, Page(s) 836

    Abstract: The coexistence of two pools of ATP synthase in mitochondria has been largely neglected despite in vitro indications for the existence of reversible active/inactive state transitions in the F1-domain of the enzyme. Herein, using cells and mitochondria ... ...

    Abstract The coexistence of two pools of ATP synthase in mitochondria has been largely neglected despite in vitro indications for the existence of reversible active/inactive state transitions in the F1-domain of the enzyme. Herein, using cells and mitochondria from mouse tissues, we demonstrate the existence in vivo of two pools of ATP synthase: one active, the other IF1-bound inactive. IF1 is required for oligomerization and inactivation of ATP synthase and for proper cristae formation. Immunoelectron microscopy shows the co-distribution of IF1 and ATP synthase, placing the inactive "sluggish" ATP synthase preferentially at cristae tips. The intramitochondrial distribution of IF1 correlates with cristae microdomains of high membrane potential, partially explaining its heterogeneous distribution. These findings support that IF1 is the in vivo regulator of the active/inactive state transitions of the ATP synthase and suggest that local regulation of IF1-ATP synthase interactions is essential to activate the sluggish ATP synthase.
    MeSH term(s) Mice ; Animals ; Mitochondrial Proton-Translocating ATPases/genetics ; Membrane Potential, Mitochondrial ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Adenosine Triphosphate/metabolism
    Chemical Substances Mitochondrial Proton-Translocating ATPases (EC 3.6.3.-) ; Adenosine Triphosphate (8L70Q75FXE)
    Language English
    Publishing date 2023-08-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-023-05214-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: An ETFDH-driven metabolon supports OXPHOS efficiency in skeletal muscle by regulating coenzyme Q homeostasis.

    Herrero Martín, Juan Cruz / Salegi Ansa, Beñat / Álvarez-Rivera, Gerardo / Domínguez-Zorita, Sonia / Rodríguez-Pombo, Pilar / Pérez, Belén / Calvo, Enrique / Paradela, Alberto / Miguez, David G / Cifuentes, Alejandro / Cuezva, José M / Formentini, Laura

    Nature metabolism

    2024  Volume 6, Issue 2, Page(s) 209–225

    Abstract: Coenzyme Q (Q) is a key lipid electron transporter, but several aspects of its biosynthesis and redox homeostasis remain undefined. Various flavoproteins reduce ubiquinone (oxidized form of Q) to ubiquinol ( ... ...

    Abstract Coenzyme Q (Q) is a key lipid electron transporter, but several aspects of its biosynthesis and redox homeostasis remain undefined. Various flavoproteins reduce ubiquinone (oxidized form of Q) to ubiquinol (QH
    MeSH term(s) Animals ; Mice ; Ubiquinone/metabolism ; Ubiquinone/therapeutic use ; Oxidative Phosphorylation ; Electron-Transferring Flavoproteins/genetics ; Electron-Transferring Flavoproteins/metabolism ; Muscle, Skeletal/metabolism ; Lipids ; Homeostasis
    Chemical Substances Ubiquinone (1339-63-5) ; Electron-Transferring Flavoproteins ; Lipids
    Language English
    Publishing date 2024-01-19
    Publishing country Germany
    Document type Journal Article
    ISSN 2522-5812
    ISSN (online) 2522-5812
    DOI 10.1038/s42255-023-00956-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: IF1 ablation prevents ATP synthase oligomerization, enhances mitochondrial ATP turnover and promotes an adenosine-mediated pro-inflammatory phenotype.

    Domínguez-Zorita, Sonia / Romero-Carramiñana, Inés / Santacatterina, Fulvio / Esparza-Moltó, Pau B / Simó, Carolina / Del-Arco, Araceli / Núñez de Arenas, Cristina / Saiz, Jorge / Barbas, Coral / Cuezva, José M

    Cell death & disease

    2023  Volume 14, Issue 7, Page(s) 413

    Abstract: ATPase Inhibitory Factor 1 (IF1) regulates the activity of mitochondrial ATP synthase. The expression of IF1 in differentiated human and mouse cells is highly variable. In intestinal cells, the overexpression of IF1 protects against colon inflammation. ... ...

    Abstract ATPase Inhibitory Factor 1 (IF1) regulates the activity of mitochondrial ATP synthase. The expression of IF1 in differentiated human and mouse cells is highly variable. In intestinal cells, the overexpression of IF1 protects against colon inflammation. Herein, we have developed a conditional IF1-knockout mouse model in intestinal epithelium to investigate the role of IF1 in mitochondrial function and tissue homeostasis. The results show that IF1-ablated mice have increased ATP synthase/hydrolase activities, leading to profound mitochondrial dysfunction and a pro-inflammatory phenotype that impairs the permeability of the intestinal barrier compromising mouse survival upon inflammation. Deletion of IF1 prevents the formation of oligomeric assemblies of ATP synthase and alters cristae structure and the electron transport chain. Moreover, lack of IF1 promotes an intramitochondrial Ca
    MeSH term(s) Animals ; Humans ; Mice ; Adenosine ; Adenosine Triphosphate ; Cell Differentiation ; Inflammation ; Mice, Knockout ; Mitochondrial Proton-Translocating ATPases/metabolism ; Mitochondrial Proteins/metabolism ; ATPase Inhibitory Protein
    Chemical Substances Adenosine (K72T3FS567) ; Adenosine Triphosphate (8L70Q75FXE) ; Atp5if1 protein, mouse ; Mitochondrial Proton-Translocating ATPases (EC 3.6.3.-) ; Mitochondrial Proteins
    Language English
    Publishing date 2023-07-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2541626-1
    ISSN 2041-4889 ; 2041-4889
    ISSN (online) 2041-4889
    ISSN 2041-4889
    DOI 10.1038/s41419-023-05957-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Analysis of the metabolic proteome of lung adenocarcinomas by reverse-phase protein arrays (RPPA) emphasizes mitochondria as targets for therapy.

    Torresano, Laura / Santacatterina, Fulvio / Domínguez-Zorita, Sonia / Nuevo-Tapioles, Cristina / Núñez-Salgado, Alfonso / Esparza-Moltó, Pau B / González-Llorente, Lucía / Romero-Carramiñana, Inés / Núñez de Arenas, Cristina / Sánchez-Garrido, Brenda / Nájera, Laura / Salas, Clara / Provencio, Mariano / Cuezva, José M

    Oncogenesis

    2022  Volume 11, Issue 1, Page(s) 24

    Abstract: Lung cancer is the leading cause of cancer-related death worldwide despite the success of therapies targeting oncogenic drivers and immune-checkpoint inhibitors. Although metabolic enzymes offer additional targets for therapy, the precise metabolic ... ...

    Abstract Lung cancer is the leading cause of cancer-related death worldwide despite the success of therapies targeting oncogenic drivers and immune-checkpoint inhibitors. Although metabolic enzymes offer additional targets for therapy, the precise metabolic proteome of lung adenocarcinomas is unknown, hampering its clinical translation. Herein, we used Reverse Phase Protein Arrays to quantify the changes in enzymes of glycolysis, oxidation of pyruvate, fatty acid metabolism, oxidative phosphorylation, antioxidant response and protein oxidative damage in 128 tumors and paired non-tumor adjacent tissue of lung adenocarcinomas to profile the proteome of metabolism. Steady-state levels of mitochondrial proteins of fatty acid oxidation, oxidative phosphorylation and of the antioxidant response are independent predictors of survival and/or of disease recurrence in lung adenocarcinoma patients. Next, we addressed the mechanisms by which the overexpression of ATPase Inhibitory Factor 1, the physiological inhibitor of oxidative phosphorylation, which is an independent predictor of disease recurrence, prevents metastatic disease. We highlight that IF1 overexpression promotes a more vulnerable and less invasive phenotype in lung adenocarcinoma cells. Finally, and as proof of concept, the therapeutic potential of targeting fatty acid assimilation or oxidation in combination with an inhibitor of oxidative phosphorylation was studied in mice bearing lung adenocarcinomas. The results revealed that this therapeutic approach significantly extended the lifespan and provided better welfare to mice than cisplatin treatments, supporting mitochondrial activities as targets of therapy in lung adenocarcinoma patients.
    Language English
    Publishing date 2022-05-09
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2674437-5
    ISSN 2157-9024
    ISSN 2157-9024
    DOI 10.1038/s41389-022-00400-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: TPL2 kinase expression is regulated by the p38γ/p38δ-dependent association of aconitase-1 with

    Escós, Alejandra / Martín-Gómez, José / González-Romero, Diego / Díaz-Mora, Ester / Francisco-Velilla, Rosario / Santiago, Cesar / Cuezva, José M / Domínguez-Zorita, Sonia / Martínez-Salas, Encarnación / Sonenberg, Nahum / Sanz-Ezquerro, Juan José / Jafarnejad, Seyed Mehdi / Cuenda, Ana

    Proceedings of the National Academy of Sciences of the United States of America

    2022  Volume 119, Issue 35, Page(s) e2204752119

    Abstract: p38γ and p38δ (p38γ/p38δ) regulate inflammation, in part by controlling tumor progression locus 2 (TPL2) expression in myeloid cells. Here, we demonstrate that TPL2 protein levels are dramatically reduced in p38γ/p38δ-deficient (p38γ/ ... ...

    Abstract p38γ and p38δ (p38γ/p38δ) regulate inflammation, in part by controlling tumor progression locus 2 (TPL2) expression in myeloid cells. Here, we demonstrate that TPL2 protein levels are dramatically reduced in p38γ/p38δ-deficient (p38γ/δ
    MeSH term(s) Aconitate Hydratase/genetics ; Aconitate Hydratase/metabolism ; Gene Expression Regulation ; Immunity, Innate ; MAP Kinase Kinase Kinases/genetics ; MAP Kinase Kinase Kinases/metabolism ; Mitogen-Activated Protein Kinase 12/genetics ; Mitogen-Activated Protein Kinase 12/metabolism ; Mitogen-Activated Protein Kinase 13/genetics ; Mitogen-Activated Protein Kinase 13/metabolism ; RNA, Messenger/genetics
    Chemical Substances RNA, Messenger ; Mitogen-Activated Protein Kinase 12 (EC 2.7.1.-) ; Mitogen-Activated Protein Kinase 13 (EC 2.7.1.-) ; MAP Kinase Kinase Kinases (EC 2.7.11.25) ; Aconitate Hydratase (EC 4.2.1.3)
    Language English
    Publishing date 2022-08-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2204752119
    Database MEDical Literature Analysis and Retrieval System OnLINE

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