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Article ; Online: From dynamin related proteins structures and oligomers to membrane fusion mediated by mitofusins.

Ozeir, Mohammad / Cohen, Mickael M

Biochimica et biophysica acta. Bioenergetics

2022 Volume 1863, Issue 8, Page(s) 148913

Abstract: Mitochondria assemble in a highly dynamic network where interconnected tubules evolve in length and size through regulated cycles of fission and fusion of mitochondrial membranes thereby adapting to cellular needs. Mitochondrial fusion and fission ... ...

Abstract	Mitochondria assemble in a highly dynamic network where interconnected tubules evolve in length and size through regulated cycles of fission and fusion of mitochondrial membranes thereby adapting to cellular needs. Mitochondrial fusion and fission processes are mediated by specific sets of mechano-chemical large GTPases that belong to the Dynamin-Related Proteins (DRPs) super family. DRPs bind to cognate membranes and auto-oligomerize to drive lipid bilayers remodeling in a nucleotide dependent manner. Although structural characterization and mechanisms of DRPs that mediate membrane fission are well established, the capacity of DRPs to mediate membrane fusion is only emerging. In this review, we discuss the distinct structures and mechanisms of DRPs that trigger the anchoring and fusion of biological membranes with a specific focus on mitofusins that are dedicated to the fusion of mitochondrial outer membranes. In particular, we will highlight oligomeric assemblies of distinct DRPs and confront their mode of action against existing models of mitofusins assemblies with emphasis on recent biochemical, structural and computational reports. As we will see, the literature brings valuable insights into the presumed macro-assemblies mitofusins may form during anchoring and fusion of mitochondrial outer membranes.
MeSH term(s)	Dynamins/chemistry ; Dynamins/metabolism ; GTP Phosphohydrolases/metabolism ; Lipid Bilayers ; Membrane Fusion ; Nucleotides
Chemical Substances	Lipid Bilayers ; Nucleotides ; GTP Phosphohydrolases (EC 3.6.1.-) ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2022-08-31
Publishing country	Netherlands
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2022.148913
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Article: From dynamin related proteins structures and oligomers to membrane fusion mediated by mitofusins

Ozeir, Mohammad / Cohen, Mickael M.

Biochimica et biophysica acta. 2022 Nov. 01, v. 1863, no. 8

2022

Abstract	Mitochondria assemble in a highly dynamic network where interconnected tubules evolve in length and size through regulated cycles of fission and fusion of mitochondrial membranes thereby adapting to cellular needs. Mitochondrial fusion and fission processes are mediated by specific sets of mechano-chemical large GTPases that belong to the Dynamin-Related Proteins (DRPs) super family. DRPs bind to cognate membranes and auto-oligomerize to drive lipid bilayers remodeling in a nucleotide dependent manner. Although structural characterization and mechanisms of DRPs that mediate membrane fission are well established, the capacity of DRPs to mediate membrane fusion is only emerging. In this review, we discuss the distinct structures and mechanisms of DRPs that trigger the anchoring and fusion of biological membranes with a specific focus on mitofusins that are dedicated to the fusion of mitochondrial outer membranes. In particular, we will highlight oligomeric assemblies of distinct DRPs and confront their mode of action against existing models of mitofusins assemblies with emphasis on recent biochemical, structural and computational reports. As we will see, the literature brings valuable insights into the presumed macro-assemblies mitofusins may form during anchoring and fusion of mitochondrial outer membranes.
Keywords	dynamins ; lipid bilayers ; mechanism of action ; membrane fusion ; mitochondria
Language	English
Dates of publication	2022-1101
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	282711-6
ISSN	0005-2728 ; 0304-4173
ISSN	0005-2728 ; 0304-4173
DOI	10.1016/j.bbabio.2022.148913
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Article ; Online: Role of Lipids and Divalent Cations in Membrane Fusion Mediated by the Heptad Repeat Domain 1 of Mitofusin.

Vlieghe, Anaïs / Niort, Kristina / Fumat, Hugo / Guigner, Jean-Michel / Cohen, Mickaël M / Tareste, David

Biomolecules

2023 Volume 13, Issue 9

Abstract: Mitochondria are highly dynamic organelles that constantly undergo fusion and fission events to maintain their shape, distribution and cellular function. Mitofusin 1 and 2 proteins are two dynamin-like GTPases involved in the fusion of outer ... ...

Abstract	Mitochondria are highly dynamic organelles that constantly undergo fusion and fission events to maintain their shape, distribution and cellular function. Mitofusin 1 and 2 proteins are two dynamin-like GTPases involved in the fusion of outer mitochondrial membranes (OMM). Mitofusins are anchored to the OMM through their transmembrane domain and possess two heptad repeat domains (HR1 and HR2) in addition to their N-terminal GTPase domain. The HR1 domain was found to induce fusion via its amphipathic helix, which interacts with the lipid bilayer structure. The lipid composition of mitochondrial membranes can also impact fusion. However, the precise mode of action of lipids in mitochondrial fusion is not fully understood. In this study, we examined the role of the mitochondrial lipids phosphatidylethanolamine (PE), cardiolipin (CL) and phosphatidic acid (PA) in membrane fusion induced by the HR1 domain, both in the presence and absence of divalent cations (Ca
MeSH term(s)	Membrane Fusion ; Cations, Divalent ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; GTP Phosphohydrolases/metabolism ; Lipids
Chemical Substances	Cations, Divalent ; GTP Phosphohydrolases (EC 3.6.1.-) ; Lipids
Language	English
Publishing date	2023-09-02
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom13091341
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Article ; Online: Recent insights into the structure and function of Mitofusins in mitochondrial fusion.

Cohen, Mickael M / Tareste, David

F1000Research

2018 Volume 7

Abstract: Mitochondria undergo frequent fusion and fission events to adapt their morphology to cellular needs. Homotypic docking and fusion of outer mitochondrial membranes are controlled by Mitofusins, a set of large membrane-anchored GTPase proteins belonging to ...

Abstract	Mitochondria undergo frequent fusion and fission events to adapt their morphology to cellular needs. Homotypic docking and fusion of outer mitochondrial membranes are controlled by Mitofusins, a set of large membrane-anchored GTPase proteins belonging to the dynamin superfamily. Mitofusins include, in addition to their GTPase and transmembrane domains, two heptad repeat domains, HR1 and HR2. All four regions are crucial for Mitofusin function, but their precise contribution to mitochondrial docking and fusion events has remained elusive until very recently. In this commentary, we first give an overview of the established strategies employed by various protein machineries distinct from Mitofusins to mediate membrane fusion. We then present recent structure-function data on Mitofusins that provide important novel insights into their mode of action in mitochondrial fusion.
MeSH term(s)	Animals ; GTP Phosphohydrolases/chemistry ; GTP Phosphohydrolases/physiology ; Humans ; Membrane Fusion ; Mitochondrial Dynamics ; Mitochondrial Membrane Transport Proteins/chemistry ; Mitochondrial Membrane Transport Proteins/physiology ; Mitochondrial Membranes/metabolism
Chemical Substances	Mitochondrial Membrane Transport Proteins ; GTP Phosphohydrolases (EC 3.6.1.-) ; Mfn1 protein, human (EC 3.6.5.-)
Language	English
Publishing date	2018-12-28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2699932-8
ISSN	2046-1402 ; 2046-1402
ISSN (online)	2046-1402
ISSN	2046-1402
DOI	10.12688/f1000research.16629.1
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Article ; Online: The dynamin-like protein Fzl promotes thylakoid fusion and resistance to light stress in Chlamydomonas reinhardtii.

Findinier, Justin / Delevoye, Cédric / Cohen, Mickael M

PLoS genetics

2019 Volume 15, Issue 3, Page(s) e1008047

Abstract: Large GTPases of the Dynamin Related Proteins (DRP) family shape lipid bilayers through membrane fission or fusion processes. Despite the highly organized photosynthetic membranes of thylakoids, a single DRP is known to be targeted inside the chloroplast. ...

Abstract	Large GTPases of the Dynamin Related Proteins (DRP) family shape lipid bilayers through membrane fission or fusion processes. Despite the highly organized photosynthetic membranes of thylakoids, a single DRP is known to be targeted inside the chloroplast. Fzl from the land plant Arabidopsis thaliana is inserted in the inner envelope and thylakoid membranes to regulate their morphology. Fzl may promote the fusion of thylakoids but this remains to be proven. Moreover, the physiological requirement for fusing thylakoids is currently unknown. Here, we find that the unicellular microalga Chlamydomonas reinhardtii encodes an Fzl ortholog (CrFzl) that is localized in the chloroplast where it is soluble. To explore its function, the CRISPR/Cas9 technology was employed to generate multiple CrFzl knock out strains. Phenotypic analyzes revealed a specific requirement of CrFzl for survival upon light stress. Consistent with this, strong irradiance lead to increased photoinhibition of photosynthesis in mutant cells. Fluorescence and electron microscopy analysis demonstrated that upon exposure to high light, CrFzl mutants show defects in chloroplast morphology but also large cytosolic vacuoles in close contact with the plastid. We further observe that strong irradiance induces an increased recruitment of the DRP to thylakoid membranes. Most importantly, we show that CrFzl is required for the fusion of thylakoids during mating. Together, our results suggest that thylakoids fusion may be necessary for resistance to light stress.
MeSH term(s)	Algal Proteins/genetics ; Algal Proteins/metabolism ; CRISPR-Cas Systems ; Chlamydomonas reinhardtii/genetics ; Chlamydomonas reinhardtii/metabolism ; Chlamydomonas reinhardtii/radiation effects ; Chloroplasts/metabolism ; Dynamins/genetics ; Dynamins/metabolism ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; Gene Knockout Techniques ; Light ; Membrane Fusion ; Microscopy, Electron, Transmission ; Mutation ; Phototrophic Processes ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Stress, Physiological ; Thylakoids/metabolism ; Thylakoids/radiation effects ; Thylakoids/ultrastructure
Chemical Substances	Algal Proteins ; Recombinant Proteins ; GTP Phosphohydrolases (EC 3.6.1.-) ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2019-03-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1008047
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Article ; Online: Mitofusin-mediated contacts between mitochondria and peroxisomes regulate mitochondrial fusion.

Alsayyah, Cynthia / Singh, Manish K / Morcillo-Parra, Maria Angeles / Cavellini, Laetitia / Shai, Nadav / Schmitt, Christine / Schuldiner, Maya / Zalckvar, Einat / Mallet, Adeline / Belgareh-Touzé, Naïma / Zimmer, Christophe / Cohen, Mickaël M

PLoS biology

2024 Volume 22, Issue 4, Page(s) e3002602

Abstract: Mitofusins are large GTPases that trigger fusion of mitochondrial outer membranes. Similarly to the human mitofusin Mfn2, which also tethers mitochondria to the endoplasmic reticulum (ER), the yeast mitofusin Fzo1 stimulates contacts between Peroxisomes ... ...

Abstract	Mitofusins are large GTPases that trigger fusion of mitochondrial outer membranes. Similarly to the human mitofusin Mfn2, which also tethers mitochondria to the endoplasmic reticulum (ER), the yeast mitofusin Fzo1 stimulates contacts between Peroxisomes and Mitochondria when overexpressed. Yet, the physiological significance and function of these "PerMit" contacts remain unknown. Here, we demonstrate that Fzo1 naturally localizes to peroxisomes and promotes PerMit contacts in physiological conditions. These contacts are regulated through co-modulation of Fzo1 levels by the ubiquitin-proteasome system (UPS) and by the desaturation status of fatty acids (FAs). Contacts decrease under low FA desaturation but reach a maximum during high FA desaturation. High-throughput genetic screening combined with high-resolution cellular imaging reveal that Fzo1-mediated PerMit contacts favor the transit of peroxisomal citrate into mitochondria. In turn, citrate enters the TCA cycle to stimulate the mitochondrial membrane potential and maintain efficient mitochondrial fusion upon high FA desaturation. These findings thus unravel a mechanism by which inter-organelle contacts safeguard mitochondrial fusion.
Language	English
Publishing date	2024-04-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.3002602
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Article ; Online: Exploring selective autophagy events in multiple biologic models using LC3-interacting regions (LIR)-based molecular traps.

Quinet, Grégoire / Génin, Pierre / Ozturk, Oznur / Belgareh-Touzé, Naima / Courtot, Lilas / Legouis, Renaud / Weil, Robert / Cohen, Mickael M / Rodriguez, Manuel S

Scientific reports

2022 Volume 12, Issue 1, Page(s) 7652

Abstract: Autophagy is an essential cellular pathway that ensures degradation of a wide range of substrates including damaged organelles or large protein aggregates. Understanding how this proteolytic pathway is regulated would increase our comprehension on its ... ...

Abstract	Autophagy is an essential cellular pathway that ensures degradation of a wide range of substrates including damaged organelles or large protein aggregates. Understanding how this proteolytic pathway is regulated would increase our comprehension on its role in cellular physiology and contribute to identify biomarkers or potential drug targets to develop more specific treatments for disease in which autophagy is dysregulated. Here, we report the development of molecular traps based in the tandem disposition of LC3-interacting regions (LIR). The estimated affinity of LC3-traps for distinct recombinant LC3/GABARAP proteins is in the low nanomolar range and allows the capture of these proteins from distinct mammalian cell lines, S. cerevisiae and C. elegans. LC3-traps show preferences for GABARAP/LGG1 or LC3/LGG2 and pull-down substrates targeted to proteaphagy and mitophagy. Therefore, LC3-traps are versatile tools that can be adapted to multiple applications to monitor selective autophagy events in distinct physiologic and pathologic circumstances.
MeSH term(s)	Animals ; Autophagy ; Caenorhabditis elegans/metabolism ; Macroautophagy ; Mammals/metabolism ; Microtubule-Associated Proteins/metabolism ; Models, Biological ; Protein Binding ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Microtubule-Associated Proteins
Language	English
Publishing date	2022-05-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-11417-z
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Article ; Online: Analysis of ATG8 Family Members Using LC3-Interacting Regions (LIR)-Based Molecular Traps.

Quinet, Grégoire / Génin, Pierre / Belgareh-Touzé, Naima / Ozturk, Oznur / Weil, Robert / Cohen, Mickael M / Legouis, Renaud / Rodriguez, Manuel S

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2602, Page(s) 191–204

Abstract: The ATG8 family of proteins regulates the autophagy process from the autophagosome maturation and cargo recruitment up to degradation. Autophagy dysfunction is involved in the development of multiple diseases. The LC3 interacting region (LIR)-based ... ...

Abstract	The ATG8 family of proteins regulates the autophagy process from the autophagosome maturation and cargo recruitment up to degradation. Autophagy dysfunction is involved in the development of multiple diseases. The LC3 interacting region (LIR)-based molecular traps have been designed to isolate endogenous ATG8 proteins and their interactors in order to facilitate the study of selective autophagy events. Here, we summarize protocols describing LC3 traps and sample preparation as well as adaptations for the analysis of ATG8 proteins in different biological models. This protocol was optimized to prepare affinity columns, reduce background, and improve the protein recovery to be analyzed by immunodetection with antibodies recognizing proteins of interest.
MeSH term(s)	Autophagy-Related Protein 8 Family/genetics ; Macroautophagy ; Acclimatization ; Antibodies ; Autophagy
Chemical Substances	Autophagy-Related Protein 8 Family ; Antibodies
Language	English
Publishing date	2022-11-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2859-1_14
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Article: The regulation of mitochondrial homeostasis by the ubiquitin proteasome system

Alsayyah, Cynthia / Ozturk, Oznur / Cavellini, Laetitia / Belgareh-Touzé, Naïma / Cohen, Mickael M

Biochimica et biophysica acta. 2020 Dec. 01, v. 1861, no. 12

2020

Abstract: From mitochondrial quality control pathways to the regulation of specific functions, the Ubiquitin Proteasome System (UPS) could be compared to a Swiss knife without which mitochondria could not maintain its integrity in the cell. Here, we review the ... ...

Abstract	From mitochondrial quality control pathways to the regulation of specific functions, the Ubiquitin Proteasome System (UPS) could be compared to a Swiss knife without which mitochondria could not maintain its integrity in the cell. Here, we review the mechanisms that the UPS employs to regulate mitochondrial function and efficiency. For this purpose, we depict how Ubiquitin and the Proteasome participate in diverse quality control pathways that safeguard entry into the mitochondrial compartment. A focus is then achieved on the UPS-mediated control of the yeast mitofusin Fzo1 which provides insights into the complex regulation of this particular protein in mitochondrial fusion. We ultimately dissect the mechanisms by which the UPS controls the degradation of mitochondria by autophagy in both mammalian and yeast systems. This organization should offer a useful overview of this abundant but fascinating literature on the crosstalks between mitochondria and the UPS.
Keywords	autophagy ; homeostasis ; mammals ; mitochondria ; proteasome endopeptidase complex ; quality control ; ubiquitin ; yeasts
Language	English
Dates of publication	2020-1201
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	282711-6
ISSN	0005-2728 ; 0304-4173
ISSN	0005-2728 ; 0304-4173
DOI	10.1016/j.bbabio.2020.148302
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: The regulation of mitochondrial homeostasis by the ubiquitin proteasome system.

Alsayyah, Cynthia / Ozturk, Oznur / Cavellini, Laetitia / Belgareh-Touzé, Naïma / Cohen, Mickael M

Biochimica et biophysica acta. Bioenergetics

2020 Volume 1861, Issue 12, Page(s) 148302

Abstract	From mitochondrial quality control pathways to the regulation of specific functions, the Ubiquitin Proteasome System (UPS) could be compared to a Swiss knife without which mitochondria could not maintain its integrity in the cell. Here, we review the mechanisms that the UPS employs to regulate mitochondrial function and efficiency. For this purpose, we depict how Ubiquitin and the Proteasome participate in diverse quality control pathways that safeguard entry into the mitochondrial compartment. A focus is then achieved on the UPS-mediated control of the yeast mitofusin Fzo1 which provides insights into the complex regulation of this particular protein in mitochondrial fusion. We ultimately dissect the mechanisms by which the UPS controls the degradation of mitochondria by autophagy in both mammalian and yeast systems. This organization should offer a useful overview of this abundant but fascinating literature on the crosstalks between mitochondria and the UPS.
MeSH term(s)	Animals ; Homeostasis ; Humans ; Mitochondria/metabolism ; Mitophagy ; Proteasome Endopeptidase Complex/metabolism ; Ubiquitin/metabolism ; Ubiquitination
Chemical Substances	Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2020-08-27
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2020.148302
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