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Article ; Online: Molecular Research on Mitochondrial Dysfunction.

Viscomi, Carlo / Soriano, Maria Eugenia

International journal of molecular sciences

2022 Volume 23, Issue 12

Abstract: This Special Issue collects current knowledge on the molecular mechanisms underlying mitochondrial dysfunction and its related diseases, as well as therapies and perspectives pertaining to their treatment [ ... ]. ...

Abstract	This Special Issue collects current knowledge on the molecular mechanisms underlying mitochondrial dysfunction and its related diseases, as well as therapies and perspectives pertaining to their treatment [...].
MeSH term(s)	Mitochondria/genetics
Language	English
Publishing date	2022-06-20
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23126845
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Article ; Online: ER Stress Priming of Mitochondrial Respiratory suPERKomplex Assembly.

Quintana-Cabrera, Ruben / Soriano, Maria Eugenia

Trends in endocrinology and metabolism: TEM

2019 Volume 30, Issue 10, Page(s) 685–687

Abstract: Assembly factors are necessary for the formation of mitochondrial supercomplexes (SCs) and in making cellular respiration more efficient. In a recent study, Balsa et al. (Mol. Cell, 2019) report that nutrient-induced endoplasmic reticulum (ER) stress ... ...

Abstract	Assembly factors are necessary for the formation of mitochondrial supercomplexes (SCs) and in making cellular respiration more efficient. In a recent study, Balsa et al. (Mol. Cell, 2019) report that nutrient-induced endoplasmic reticulum (ER) stress engages PERK-eIF2α-mediated transcription of the SCs assembly factor SCAF1, events that coordinate ER stress and SCs formation to improve bioenergetics.
MeSH term(s)	Electron Transport ; Endoplasmic Reticulum Stress ; Eukaryotic Initiation Factor-2 ; Nutrients ; Signal Transduction ; eIF-2 Kinase
Chemical Substances	Eukaryotic Initiation Factor-2 ; eIF-2 Kinase (EC 2.7.11.1)
Language	English
Publishing date	2019-08-24
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	1042384-9
ISSN	1879-3061 ; 1043-2760
ISSN (online)	1879-3061
ISSN	1043-2760
DOI	10.1016/j.tem.2019.08.003
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Zs.A 2999: Show issues

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Article ; Online: NOX2 and NOX4 control mitochondrial function in chronic myeloid leukaemia.

Romo-González, Marta / Ijurko, Carla / Alonso, María Teresa / Gómez de Cedrón, Marta / Ramirez de Molina, Ana / Soriano, María Eugenia / Hernández-Hernández, Ángel

Free radical biology & medicine

2023 Volume 198, Page(s) 92–108

Abstract: Cancer cells are characterised by an elevated metabolic plasticity and enhanced production of reactive oxygen species (ROS), two features acknowledged as hallmarks in cancer, with a high translational potential to the therapeutic setting. These aspects, ... ...

Abstract	Cancer cells are characterised by an elevated metabolic plasticity and enhanced production of reactive oxygen species (ROS), two features acknowledged as hallmarks in cancer, with a high translational potential to the therapeutic setting. These aspects, that have been traditionally studied separately, are in fact intimately intermingled. As part of their transforming activity, some oncogenes stimulate rewiring of metabolic processes, whilst simultaneously promoting increased production of intracellular ROS. In this scenario the latest discoveries suggest the relevance of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases (NOX) to connect ROS production and metabolic control. Here we have analysed the relevance of NOX2 and NOX4 in the regulation of metabolism in chronic myeloid leukaemia (CML), a neoplasia driven by the expression of the breakpoint cluster region-Abelson fusion oncogene (BCR-ABL). Silencing of NOX2 enhances glycolysis and oxidative phosphorylation rates, together with an enhanced production of mitochondrial ROS and a decrease in mitochondrial DNA copy number, which reflects mitochondrial dysfunction. NOX4 expression was upregulated upon NOX2 silencing, and this was required to alter mitochondrial function. Our results support the relevance of NOX2 to regulate metabolism-related signalling pathways downstream of BCR-ABL. Overall we show that NOX2, through the regulation of NOX4 expression, controls metabolism and mitochondrial function in CML cells. This notion was confirmed by transcriptomic analyses, that strongly relate both NOX isoforms with metabolism regulation in CML.
MeSH term(s)	Humans ; Reactive Oxygen Species/metabolism ; NADPH Oxidase 2 ; NADPH Oxidase 4 ; NADPH Oxidases/metabolism ; Leukemia, Myeloid ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive ; Mitochondria/metabolism
Chemical Substances	Reactive Oxygen Species ; NADPH Oxidase 2 (EC 1.6.3.-) ; NADPH Oxidase 4 (EC 1.6.3.-) ; NADPH Oxidases (EC 1.6.3.-) ; NOX4 protein, human (EC 1.6.3.-)
Language	English
Publishing date	2023-02-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2023.02.005
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Zs.A 2109: Show issues

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Article ; Online: Traveling Bax and forth from mitochondria to control apoptosis.

Soriano, Maria Eugenia / Scorrano, Luca

Cell

2011 Volume 145, Issue 1, Page(s) 15–17

Abstract: Antiapoptotic Bcl-2 proteins on mitochondria inhibit prodeath proteins, such as Bax, which are found primarily in the cytosol. In this issue, Edlich et al., (2011) show that Bax and Bcl-xL interact on the mitochondrial surface and then retrotranslocate ... ...

Abstract	Antiapoptotic Bcl-2 proteins on mitochondria inhibit prodeath proteins, such as Bax, which are found primarily in the cytosol. In this issue, Edlich et al., (2011) show that Bax and Bcl-xL interact on the mitochondrial surface and then retrotranslocate to the cytosol, effectively preventing Bax-induced permeabilization of mitochondria.
Language	English
Publishing date	2011-03-31
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2011.03.025
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Zs.A 1167: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 58: Show issues

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Article ; Online: Regulation of Mitochondrial Electron Transport Chain Assembly.

Cogliati, Sara / Lorenzi, Isotta / Rigoni, Giovanni / Caicci, Federico / Soriano, Maria Eugenia

Journal of molecular biology

2018 Volume 430, Issue 24, Page(s) 4849–4873

Abstract: Mitochondrial function depends on the correct synthesis, transport, and assembly of proteins and cofactors of the electron transport chain. The initial idea that the respiratory chain protein complexes (RCCs) were independent structures in the inner ... ...

Abstract	Mitochondrial function depends on the correct synthesis, transport, and assembly of proteins and cofactors of the electron transport chain. The initial idea that the respiratory chain protein complexes (RCCs) were independent structures in the inner mitochondrial membrane evolved after the identification of higher quaternary structures called supercomplexes (SCs), whose formation is dynamically regulated in order to accommodate cellular metabolic demands. Due to the dual genetic origin of the mitochondrial proteome, electron transport chain and SCs formation must be tightly regulated to coordinate the expression and assembly of components encoded by both genomes. This regulation occurs at different levels from gene transcription to protein, complex or SCs assembly, and might involve the participation of factors that contribute to the formation and stability of the RCCs and SCs. Here we review the cellular pathways and assembly factors that regulate RCCs and SCs formation.
MeSH term(s)	Animals ; Electron Transport ; Evolution, Molecular ; Gene Expression Regulation ; Humans ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/metabolism ; Oxidative Phosphorylation ; Phylogeny
Chemical Substances	Mitochondrial Proteins ; Multienzyme Complexes
Language	English
Publishing date	2018-10-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2018.09.016
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Zs.A 867: Show issues

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Article: The interplay between BCL-2 family proteins and mitochondrial morphology in the regulation of apoptosis.

Soriano, Maria Eugenia / Scorrano, Luca

Advances in experimental medicine and biology

2010 Volume 687, Page(s) 97–114

Abstract: Apoptosis is a highly regulated process where key players such as BCL-2 family members control the recruitment of the mitochondrial subroutine. This culminates in the release of cytochrome c from the organelle in the cytoplasm, where it is required for ... ...

Abstract	Apoptosis is a highly regulated process where key players such as BCL-2 family members control the recruitment of the mitochondrial subroutine. This culminates in the release of cytochrome c from the organelle in the cytoplasm, where it is required for the activation of effector caspases. The complete release of cytochrome c is the result of the combined action of proapoptotic BCL-2 family members and of changes in the complex morphology and ultrastructure of the organelle, controlled by the balance between fusion and fission processes. Here we discuss recent findings pointing to a role for changes in mitochondrial morphology during apoptosis and how these might be regulated by members of the BCL-2 family.
MeSH term(s)	Animals ; Apoptosis/physiology ; History, 20th Century ; Humans ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Myeloid Cell Leukemia Sequence 1 Protein ; Proto-Oncogene Proteins c-bcl-2/genetics ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Signal Transduction/physiology ; bcl-X Protein/genetics ; bcl-X Protein/metabolism
Chemical Substances	Myeloid Cell Leukemia Sequence 1 Protein ; Proto-Oncogene Proteins c-bcl-2 ; bcl-X Protein
Language	English
Publishing date	2010-10-03
Publishing country	United States
Document type	Historical Article ; Journal Article ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-1-4419-6706-0_6
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Article ; Online: OPA1 drives macrophage metabolism and functional commitment via p65 signaling.

Sánchez-Rodríguez, Ricardo / Tezze, Caterina / Agnellini, Andrielly H R / Angioni, Roberta / Venegas, Francisca C / Cioccarelli, Chiara / Munari, Fabio / Bertoldi, Nicole / Canton, Marcella / Desbats, Maria Andrea / Salviati, Leonardo / Gissi, Rosanna / Castegna, Alessandra / Soriano, Maria Eugenia / Sandri, Marco / Scorrano, Luca / Viola, Antonella / Molon, Barbara

Cell death and differentiation

2022 Volume 30, Issue 3, Page(s) 742–752

Abstract: Macrophages are essential players for the host response against pathogens, regulation of inflammation and tissue regeneration. The wide range of macrophage functions rely on their heterogeneity and plasticity that enable a dynamic adaptation of their ... ...

Abstract	Macrophages are essential players for the host response against pathogens, regulation of inflammation and tissue regeneration. The wide range of macrophage functions rely on their heterogeneity and plasticity that enable a dynamic adaptation of their responses according to the surrounding environmental cues. Recent studies suggest that metabolism provides synergistic support for macrophage activation and elicitation of desirable immune responses; however, the metabolic pathways orchestrating macrophage activation are still under scrutiny. Optic atrophy 1 (OPA1) is a mitochondria-shaping protein controlling mitochondrial fusion, cristae biogenesis and respiration; clear evidence shows that the lack or dysfunctional activity of this protein triggers the accumulation of metabolic intermediates of the TCA cycle. In this study, we show that OPA1 has a crucial role in macrophage activation. Selective Opa1 deletion in myeloid cells impairs M1-macrophage commitment. Mechanistically, Opa1 deletion leads to TCA cycle metabolite accumulation and defective NF-κB signaling activation. In an in vivo model of muscle regeneration upon injury, Opa1 knockout macrophages persist within the damaged tissue, leading to excess collagen deposition and impairment in muscle regeneration. Collectively, our data indicate that OPA1 is a key metabolic driver of macrophage functions.
MeSH term(s)	Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Signal Transduction ; Macrophages/metabolism
Language	English
Publishing date	2022-10-28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1225672-9
ISSN	1476-5403 ; 1350-9047
ISSN (online)	1476-5403
ISSN	1350-9047
DOI	10.1038/s41418-022-01076-y
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Zs.A 4230: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 80: Show issues

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Article ; Online: A new split-GFP-based probe reveals DJ-1 translocation into the mitochondrial matrix to sustain ATP synthesis upon nutrient deprivation.

Calì, Tito / Ottolini, Denis / Soriano, Maria Eugenia / Brini, Marisa

Human molecular genetics

2015 Volume 24, Issue 4, Page(s) 1045–1060

Abstract: The Parkinson's disease-related protein DJ-1 has a role in the protection against oxidative stress and maintenance of mitochondria structure. Whether this action depends on its localization and activity within the mitochondria is not clear. Here we ... ...

Abstract	The Parkinson's disease-related protein DJ-1 has a role in the protection against oxidative stress and maintenance of mitochondria structure. Whether this action depends on its localization and activity within the mitochondria is not clear. Here we develop an approach to resolve intra-mitochondrial distribution of DJ-1 and monitor its translocation under specific conditions. By a new split-green fluorescent protein (GFP)-based tool, we can observe that a small DJ-1 fraction is located within the mitochondrial matrix and that it consistently increases upon nutrient depletion. We also find that the targeting of DJ-1 to the mitochondrial matrix enhances mitochondrial and cytosolic adenosine triphosphate levels. Intriguingly, DJ-1 pathogenic mutants fail to improve bioenergetics and translocate within the mitochondrial matrix, suggesting that the DJ-1 protective role requires both these actions. By this new split-GFP-based tool, we can resolve mitochondrial compartmentalization of proteins which are not constitutively resident in mitochondria but translocate to them in response to specific stimuli.
MeSH term(s)	Adenosine Triphosphate/biosynthesis ; Autophagy/genetics ; Cell Line ; Cytoplasm/metabolism ; Gene Expression ; Humans ; Intracellular Signaling Peptides and Proteins/chemistry ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Mitochondria/genetics ; Mitochondria/metabolism ; Models, Molecular ; Mutation ; Oncogene Proteins/chemistry ; Oncogene Proteins/genetics ; Oncogene Proteins/metabolism ; Protein Conformation ; Protein Deglycase DJ-1 ; Protein Transport
Chemical Substances	Intracellular Signaling Peptides and Proteins ; Oncogene Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; PARK7 protein, human (EC 3.1.2.-) ; Protein Deglycase DJ-1 (EC 3.1.2.-)
Language	English
Publishing date	2015-02-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddu519
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Zs.A 3469: Show issues

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Article: PARP Inhibitor PJ34 Protects Mitochondria and Induces DNA-Damage Mediated Apoptosis in Combination With Cisplatin or Temozolomide in B16F10 Melanoma Cells.

Cseh, Anna Maria / Fabian, Zsolt / Quintana-Cabrera, Ruben / Szabo, Aliz / Eros, Krisztian / Soriano, Maria Eugenia / Gallyas, Ferenc / Scorrano, Luca / Sumegi, Balazs

Frontiers in physiology

2019 Volume 10, Page(s) 538

Abstract: PARP-1 inhibition has recently been employed in both mono- and combination therapies in various malignancies including melanoma with both promising and contradicting results reported. Although deeper understanding of the underlying molecular mechanisms ... ...

Abstract	PARP-1 inhibition has recently been employed in both mono- and combination therapies in various malignancies including melanoma with both promising and contradicting results reported. Although deeper understanding of the underlying molecular mechanisms may help improving clinical modalities, the complex cellular effects of PARP inhibitors make disentangling of the mechanisms involved in combination therapies difficult. Here, we used two cytostatic agents used in melanoma therapies in combination with PARP inhibition to have an insight into cellular events using the B16F10 melanoma model. We found that, when used in combination with cisplatin or temozolomide, pharmacologic blockade of PARP-1 by PJ34 augmented the DNA-damaging and cytotoxic effects of both alkylating compounds. Interestingly, however, this synergism unfolds relatively slowly and is preceded by molecular events that are traditionally believed to support cell survival including the stabilization of mitochondrial membrane potential and morphology. Our data indicate that the PARP inhibitor PJ34 has, apparently, opposing effects on the mitochondrial structure and cell survival. While, initially, it stimulates mitochondrial fusion and hyperpolarization, hallmarks of mitochondrial protection, it enhances the cytotoxic effects of alkylating agents at later stages. These findings may contribute to the optimization of PARP inhibitor-based antineoplastic modalities.
Language	English
Publishing date	2019-05-07
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2564217-0
ISSN	1664-042X
ISSN	1664-042X
DOI	10.3389/fphys.2019.00538
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Article ; Online: The displacement of frataxin from the mitochondrial cristae correlates with abnormal respiratory supercomplexes formation and bioenergetic defects in cells of Friedreich ataxia patients.

Doni, Davide / Rigoni, Giovanni / Palumbo, Elisa / Baschiera, Elisa / Peruzzo, Roberta / De Rosa, Edith / Caicci, Federico / Passerini, Leonardo / Bettio, Daniela / Russo, Antonella / Szabò, Ildiko / Soriano, Maria Eugenia / Salviati, Leonardo / Costantini, Paola

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2021 Volume 35, Issue 3, Page(s) e21362

Abstract: Friedreich ataxia (FRDA) is a neurodegenerative disease resulting from a severe decrease of frataxin (FXN). Most patients carry a GAA repeat expansion in both alleles of the FXN gene, whereas a small fraction of them are compound heterozygous for the ... ...

Abstract	Friedreich ataxia (FRDA) is a neurodegenerative disease resulting from a severe decrease of frataxin (FXN). Most patients carry a GAA repeat expansion in both alleles of the FXN gene, whereas a small fraction of them are compound heterozygous for the expansion and a point mutation in the other allele. FXN is involved in the mitochondrial biogenesis of the FeS-clusters. Distinctive feature of FRDA patient cells is an impaired cellular respiration, likely due to a deficit of key redox cofactors working as electrons shuttles through the respiratory chain. However, a definite relationship between FXN levels, FeS-clusters assembly dysregulation and bioenergetics failure has not been established. In this work, we performed a comparative analysis of the mitochondrial phenotype of cell lines from FRDA patients, either homozygous for the expansion or compound heterozygotes for the G130V mutation. We found that, in healthy cells, FXN and two key proteins of the FeS-cluster assembly machinery are enriched in mitochondrial cristae, the dynamic subcompartment housing the respiratory chain. On the contrary, FXN widely redistributes to the matrix in FRDA cells with defects in respiratory supercomplexes assembly and altered respiratory function. We propose that this could be relevant for the early mitochondrial defects afflicting FRDA cells and that perturbation of mitochondrial morphodynamics could in turn be critical in terms of disease mechanisms.
MeSH term(s)	Cell Line ; Electron Transport Chain Complex Proteins/biosynthesis ; Energy Metabolism ; Friedreich Ataxia/metabolism ; Friedreich Ataxia/pathology ; Humans ; Iron-Binding Proteins/genetics ; Iron-Binding Proteins/physiology ; Mitochondrial Membranes/metabolism ; Mitochondrial Membranes/pathology ; Frataxin
Chemical Substances	Electron Transport Chain Complex Proteins ; Iron-Binding Proteins
Language	English
Publishing date	2021-02-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.202000524RR
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Zs.A 2266: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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