The desmin network is a determinant of the cytoplasmic stiffness of myoblasts

Charrier, Elisabeth E.; Montel, Lorraine; Asnacios, Atef; Delort, Florence; Vicart, Patrick; Gallet, François; Batonnet-Pichon, Sabrina; Hénon, Sylvie

doi:10.1111/boc.201700040

Cited by 31 publications

(23 citation statements)

References 53 publications

(91 reference statements)

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“…Consistent with the high degree of strain stiffening in IF networks, softening due to loss of vimentin is more evident at large cell deformations, especially in response to compression (Mendez et al, 2014). Similarly, loss of desmin has little effect on the stiffness of the myocyte cortex at small deformations, but is important for whole-cell stiffness at large strains (Charrier et al, 2018).…”

Section: Mechanical Properties Of If Networkmentioning

confidence: 62%

Scaling up single-cell mechanics to multicellular tissues – the role of the intermediate filament–desmosome network

Broussard

Jaiganesh

Zarkoob

et al. 2020

Journal of Cell Science

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Cells and tissues sense, respond to and translate mechanical forces into biochemical signals through mechanotransduction, which governs individual cell responses that drive gene expression, metabolic pathways and cell motility, and determines how cells work together in tissues. Mechanotransduction often depends on cytoskeletal networks and their attachment sites that physically couple cells to each other and to the extracellular matrix. One way that cells associate with each other is through Ca 2+-dependent adhesion molecules called cadherins, which mediate cell-cell interactions through adherens junctions, thereby anchoring and organizing the cortical actin cytoskeleton. This actin-based network confers dynamic properties to cell sheets and developing organisms. However, these contractile networks do not work alone but in concert with other cytoarchitectural elements, including a diverse network of intermediate filaments. This Review takes a close look at the intermediate filament network and its associated intercellular junctions, desmosomes. We provide evidence that this system not only ensures tissue integrity, but also cooperates with other networks to create more complex tissues with emerging properties in sensing and responding to increasingly stressful environments. We will also draw attention to how defects in intermediate filament and desmosome networks result in both chronic and acquired diseases.

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Section: Mechanical Properties Of If Networkmentioning

confidence: 62%

Scaling up single-cell mechanics to multicellular tissues – the role of the intermediate filament–desmosome network

Broussard

Jaiganesh

Zarkoob

et al. 2020

Journal of Cell Science

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“…In contrast to longitudinal, permeabilized fiber transverse stiffness depends to a lesser degree on intact titin, which is responsible for approximately one third of this stiffness. Other contributors to myocyte stiffness, especially transverse compressive stiffness, may include the microtubules (Kerr et al, 2015), the desmin intermediate filaments (Charrier et al, 2018), and the non-sarcomeric actin filament (microfilament) network (Wang et al, 2009). Glycerol permeabilization procedures on fibers (performed in the current work) degrade some, but not all, of these extramyofibrillar structures, and so their contributions to fiber stiffness will probably be greater for intact fibers or whole muscles (Brynnel et al, 2018; Irving et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Graded titin cleavage progressively reduces tension and uncovers the source of A-band stability in contracting muscle

Li¹,

Hessel²,

Unger³

et al. 2020

Preprint

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The giant muscle protein titin is a major contributor to passive force; however, its role in active force generation is unresolved. Here, we use a novel titin-cleavage (TC) mouse model that allows specific and rapid cutting of elastic titin to quantify how titin-based forces define myocyte ultrastructure and mechanics. We show that under mechanical strain, as titin cleavage doubles from heterozygous to homozygous TC muscles, Z-disks become increasingly out of register while passive and active forces are reduced. Interactions of elastic titin with sarcomeric actin filaments are revealed. Strikingly, when titin-cleaved muscles contract, myosin-containing A-bands become split and adjacent myosin filaments move in opposite directions while also shedding myosins. This establishes intact titin filaments as critical force-transmission networks, buffering the forces observed by myosin filaments during contraction. To perform this function, elastic titin must change stiffness or extensible length, unveiling its fundamental role as an activation-dependent spring in contracting muscle.

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“…The correlation between stress and strain depends on the mechanical properties of the cell. The local techniques, involving magnetic and optical tweezers, allow for local and global deformation, with magnetic tweezers reaching higher forces (in the tens of nN range) than optical tweezers (less than 100 pN), and lead to similar viscoelastic moduli values [145][146][147][148]. The other setups allow deformation of the entire cell ( Figure 2B).…”

Section: Powerful Tools For Assessing Cell Mechanicanical Properties mentioning

confidence: 99%

Molecular and Mechanobiological Pathways Related to the Physiopathology of FPLD2

Varlet

Helfer

Badens

2020

Cells

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Laminopathies are rare and heterogeneous diseases affecting one to almost all tissues, as in Progeria, and sharing certain features such as metabolic disorders and a predisposition to atherosclerotic cardiovascular diseases. These two features are the main characteristics of the adipose tissue-specific laminopathy called familial partial lipodystrophy type 2 (FPLD2). The only gene that is involved in FPLD2 physiopathology is the LMNA gene, with at least 20 mutations that are considered pathogenic. LMNA encodes the type V intermediate filament lamin A/C, which is incorporated into the lamina meshwork lining the inner membrane of the nuclear envelope. Lamin A/C is involved in the regulation of cellular mechanical properties through the control of nuclear rigidity and deformability, gene modulation and chromatin organization. While recent studies have described new potential signaling pathways dependent on lamin A/C and associated with FPLD2 physiopathology, the whole picture of how the syndrome develops remains unknown. In this review, we summarize the signaling pathways involving lamin A/C that are associated with the progression of FPLD2. We also explore the links between alterations of the cellular mechanical properties and FPLD2 physiopathology. Finally, we introduce potential tools based on the exploration of cellular mechanical properties that could be redirected for FPLD2 diagnosis.

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The desmin network is a determinant of the cytoplasmic stiffness of myoblasts

Cited by 31 publications

References 53 publications

Scaling up single-cell mechanics to multicellular tissues – the role of the intermediate filament–desmosome network

Scaling up single-cell mechanics to multicellular tissues – the role of the intermediate filament–desmosome network

Graded titin cleavage progressively reduces tension and uncovers the source of A-band stability in contracting muscle

Molecular and Mechanobiological Pathways Related to the Physiopathology of FPLD2

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