Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo

Rouyère, Clémentine; Serrano, Thomas; Frémont, Stéphane; Échard, Arnaud

doi:10.1016/j.ejcb.2022.151249

Cited by 47 publications

(42 citation statements)

References 185 publications

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“…Cys374 on actin is highly reactive and probably the most redox-sensitive cysteine (Lassing et al , 2007). Cysteine oxidation can cause the formation of intra- or inter-molecular disulfide bridges (Farah et al , 2011; Balta et al , 2021; Rouyère et al , 2022) that impairs actin polymerization (DalleDonne et al , 1995, 1999). As one of the intermediates during nucleotide exchange is nucleotide-free actin which is very unstable unless stabilized by sucrose (De La Cruz & Pollard, 1995), it can be thought that the repetition of cycles during turnover may induce its degradation.…”

Section: Discussionmentioning

confidence: 99%

“…It is also possible that during these successive cycles, actin becomes more sensitive to ROS. Cells may have overcome these issues with systems of chaperones (Dalle-Donne et al , 2001; Wettstein et al , 2012; Grantham, 2020), by having an effective system of protein synthesis and degradation to maintain a pool of polymerizable actin monomers (Olson & Nordheim, 2010; Vedula et al , 2021) or by limiting oxidative stress (Rouyère et al , 2022).…”

Section: Discussionmentioning

confidence: 99%

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Recycling limits the lifetime of actin turnover

Blanchoin

Théry

Colin

et al. 2022

Preprint

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Intracellular organization is largely mediated by the actin turnover. Cellular actin networks consume matter and energy to sustain their dynamics, while maintaining their appearance. This behavior, called 'dynamic steady state', enables cells to sense and adapt to their environment. However, how structural stability can be maintained during the constant turnover of a limited actin monomer pool is poorly understood. To answer this question, we developed an experimental system using actin bead motility in a cell-sized compartment with a limited amount of monomer. We used the speed and the size of the actin comet tails to evaluate the system's monomer consumption and its lifetime. We established the relative contribution of actin assembly, disassembly and recycling for a bead movement over tens of hours. Recycling mediated by cyclase-associated proteins is the key step in allowing the reuse of monomers for multiple assembly cycles. Energy supply and protein aging are also factors that limit the lifetime of actin turnover. This work reveals the balancing mechanism for long-term network assembly with a limited amount of building blocks.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Recycling limits the lifetime of actin turnover

Blanchoin

Théry

Colin

et al. 2022

Preprint

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“…That work (Terman et al, 2002) also identified multiple different MICAL genes and that they comprise a family of phylogenetically-conserved proteins with one member in Drosophila (called Mical) and three in vertebrates, including humans [named MICAL-1, MICAL-2, and MICAL-3 (or also known as MICAL1, MICAL2, and MICAL3)] (Figure 1A). MICALs are large proteins (>1,000 amino acids) consisting of a highly conserved N-terminal flavoprotein monooxygenase (also called hydroxylase, MO, FM, or Redox) domain, followed by several other notable regions, including a calponin homology (CH) domain, a Lin-11, Isl-1, Mec-3 (LIM) domain, a proline-rich region with PxxP ligands for SH3-domain containing proteins, and a region that shares homology to the alpha (α) region of Ezrin, Radixin, and Moesin (ERM) proteins (this region is now often referred to as the Plexin-interacting region (PIR), Rab binding domain (RBD), bMERB, or CC) [Figure 1A (Terman et al, 2002;Alto and Terman, 2018;Rouyère et al, 2022)]. Each MICAL family member, including those in Drosophila and humans, has multiple different splice forms/isoforms (Terman et al, 2002), which impact their enzymatic and cellular functions [Figure 1A; e.g., (Terman et al, 2002;Weide et al, 2003;Pasterkamp et al, 2006;Wilson et al, 2016;Rouyère et al, 2022)].…”

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confidence: 99%

MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics

Rajan

Terman

Reisler

2023

Front. Cell Dev. Biol.

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Actin and its dynamic structural remodelings are involved in multiple cellular functions, including maintaining cell shape and integrity, cytokinesis, motility, navigation, and muscle contraction. Many actin-binding proteins regulate the cytoskeleton to facilitate these functions. Recently, actin’s post-translational modifications (PTMs) and their importance to actin functions have gained increasing recognition. The MICAL family of proteins has emerged as important actin regulatory oxidation-reduction (Redox) enzymes, influencing actin’s properties both in vitro and in vivo. MICALs specifically bind to actin filaments and selectively oxidize actin’s methionine residues 44 and 47, which perturbs filaments’ structure and leads to their disassembly. This review provides an overview of the MICALs and the impact of MICAL-mediated oxidation on actin’s properties, including its assembly and disassembly, effects on other actin-binding proteins, and on cells and tissue systems.

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“…The effects could be reversed fully by using antioxidants and partly by supplementing PKA. Also, specific oxidations of actin or titin have been associated with development of heart diseases [121,122].…”

Section: Sarcomeric Dysfunctionmentioning

confidence: 99%

Cardiomyopathies in Children: Genetics, Pathomechanisms and Therapeutic Strategies

Cimiotti¹,

Sadat-Ebrahimi²,

Mügge³

et al. 2024

New Insights on Cardiomyopathy

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Despite great advances in cardiovascular medicine, cardiomyopathies in children still are challenging for pediatricians as well as cardiologists. Pediatric cardiomyopathies can manifest in diverse phenotypes but are often life-threatening and have a poor prognosis. However, many therapeutic options available for adult patients do not apply for children, leaving a very limited portfolio to attenuate disease progression to avoid or postpone heart transplantation. Childhood cardiomyopathies can arise from different etiologies, but genetic defects such as mutations, for example, in sarcomeric proteins, which are pivotal for the contractile function, are common. This leads to the demand to identify new variants found by genetic screening as pathogenic and furthermore to allow a prognosis or risk assessment for related carriers, thus increasing the need to uncover molecular pathomechanisms of such mutations. This chapter aims to highlight the unique characteristics of pediatric cardiomyopathies in contrast to adult forms, including etiology, pathophysiology, genetics, as well as molecular mechanisms. We will also tackle currents options, challenges, and perspectives in diagnosis and treatment of pediatric cardiomyopathies.

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Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo

Cited by 47 publications

References 185 publications

Recycling limits the lifetime of actin turnover

Recycling limits the lifetime of actin turnover

MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics

Cardiomyopathies in Children: Genetics, Pathomechanisms and Therapeutic Strategies

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