Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo
Actin is among the most abundant proteins in eukaryotic cells and assembles into dynamic filamentous networks regulated by many actin binding proteins. The actin cytoskeleton must be finely tuned, both in space and time, to fulfill key cellular functions such as cell division, cell shape changes, ph...
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| Format: | Article |
| Language: | English |
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Elsevier
2022-06-01
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| Series: | European Journal of Cell Biology |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0171933522000528 |
| _version_ | 1828294407513702400 |
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| author | Clémentine Rouyère Thomas Serrano Stéphane Frémont Arnaud Echard |
| author_facet | Clémentine Rouyère Thomas Serrano Stéphane Frémont Arnaud Echard |
| author_sort | Clémentine Rouyère |
| collection | DOAJ |
| description | Actin is among the most abundant proteins in eukaryotic cells and assembles into dynamic filamentous networks regulated by many actin binding proteins. The actin cytoskeleton must be finely tuned, both in space and time, to fulfill key cellular functions such as cell division, cell shape changes, phagocytosis and cell migration. While actin oxidation by reactive oxygen species (ROS) at non-physiological levels are known for long to impact on actin polymerization and on the cellular actin cytoskeleton, growing evidence shows that direct and reversible oxidation/reduction of specific actin amino acids plays an important and physiological role in regulating the actin cytoskeleton. In this review, we describe which actin amino acid residues can be selectively oxidized and reduced in many different ways (e.g. disulfide bond formation, glutathionylation, carbonylation, nitration, nitrosylation and other oxidations), the cellular enzymes at the origin of these post-translational modifications, and the impact of actin redox modifications both in vitro and in vivo. We show that the regulated balance of oxidation and reduction of key actin amino acid residues contributes to the control of actin filament polymerization and disassembly at the subcellular scale and highlight how improper redox modifications of actin can lead to pathological conditions. |
| first_indexed | 2024-04-13T11:37:06Z |
| format | Article |
| id | doaj.art-2503c34ec30d47cfb7a79c2326e0677b |
| institution | Directory Open Access Journal |
| issn | 0171-9335 |
| language | English |
| last_indexed | 2024-04-13T11:37:06Z |
| publishDate | 2022-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | European Journal of Cell Biology |
| spelling | doaj.art-2503c34ec30d47cfb7a79c2326e0677b2022-12-22T02:48:25ZengElsevierEuropean Journal of Cell Biology0171-93352022-06-011013151249Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivoClémentine Rouyère0Thomas Serrano1Stéphane Frémont2Arnaud Echard3Institut Pasteur, Université Paris Cité, CNRS UMR3691, Membrane Traffic and Cell Division Unit, 25–28 rue du Dr Roux, F-75015 Paris, France; Sorbonne Université, Collège Doctoral, F-75005 Paris, FranceInstitut Pasteur, Université Paris Cité, CNRS UMR3691, Membrane Traffic and Cell Division Unit, 25–28 rue du Dr Roux, F-75015 Paris, FranceInstitut Pasteur, Université Paris Cité, CNRS UMR3691, Membrane Traffic and Cell Division Unit, 25–28 rue du Dr Roux, F-75015 Paris, FranceInstitut Pasteur, Université Paris Cité, CNRS UMR3691, Membrane Traffic and Cell Division Unit, 25–28 rue du Dr Roux, F-75015 Paris, France; Corresponding author.Actin is among the most abundant proteins in eukaryotic cells and assembles into dynamic filamentous networks regulated by many actin binding proteins. The actin cytoskeleton must be finely tuned, both in space and time, to fulfill key cellular functions such as cell division, cell shape changes, phagocytosis and cell migration. While actin oxidation by reactive oxygen species (ROS) at non-physiological levels are known for long to impact on actin polymerization and on the cellular actin cytoskeleton, growing evidence shows that direct and reversible oxidation/reduction of specific actin amino acids plays an important and physiological role in regulating the actin cytoskeleton. In this review, we describe which actin amino acid residues can be selectively oxidized and reduced in many different ways (e.g. disulfide bond formation, glutathionylation, carbonylation, nitration, nitrosylation and other oxidations), the cellular enzymes at the origin of these post-translational modifications, and the impact of actin redox modifications both in vitro and in vivo. We show that the regulated balance of oxidation and reduction of key actin amino acid residues contributes to the control of actin filament polymerization and disassembly at the subcellular scale and highlight how improper redox modifications of actin can lead to pathological conditions.http://www.sciencedirect.com/science/article/pii/S0171933522000528ActinRedoxMICALMsrBOxidoreductase |
| spellingShingle | Clémentine Rouyère Thomas Serrano Stéphane Frémont Arnaud Echard Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo European Journal of Cell Biology Actin Redox MICAL MsrB Oxidoreductase |
| title | Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo |
| title_full | Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo |
| title_fullStr | Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo |
| title_full_unstemmed | Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo |
| title_short | Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo |
| title_sort | oxidation and reduction of actin origin impact in vitro and functional consequences in vivo |
| topic | Actin Redox MICAL MsrB Oxidoreductase |
| url | http://www.sciencedirect.com/science/article/pii/S0171933522000528 |
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