Specific attachment of desmin filaments to desmosomal plaques in cardiac myocytes.

Kartenbeck, Jürgen; Franke, Werner W.; Moser, Jürgen; Stoffels, U.

doi:10.1002/j.1460-2075.1983.tb01493.x

Cited by 117 publications

(80 citation statements)

References 52 publications

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“…Hence, we first investigated the localization of DP and desmin in longitudinal sections of monkey cardiac muscle by double immunofluorescence microscopy. As expected (Kartenbeck et al, 1983), these two proteins were both found at the level of intercalated discs. Desmin also showed the typical cross-striated labeling in a distinct sarcomeric pattern (Fig.…”

Section: Resultssupporting

confidence: 82%

“…Ultrastructural studies have shown that desmin filaments attach in a lateral fashion to the DP-containing region of the desmosomal plaques of the heart, which suggests that special domains exist in desmin that are involved in binding (Kartenbeck et al, 1983). Recent immunoelectron microscopy studies have revealed that, at intercalated discs, desmosomes and fasciae adherentes form a highly integrated system, for which the term of area composita has been proposed (Franke et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

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New insights into the molecular basis of desmoplakinand desmin-related cardiomyopathies

Lapouge

Fontao

Champliaud

et al. 2006

Journal of Cell Science

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Desmosomes are intercellular adhesive complexes that anchor the intermediate filament cytoskeleton to the cell membrane in epithelia and cardiac muscle cells. The desmosomal component desmoplakin plays a key role in tethering various intermediate filament networks through its C-terminal plakin repeat domain. To gain better insight into the cytoskeletal organization of cardiomyocytes, we investigated the association of desmoplakin with desmin by cell transfection, yeast two-hybrid, and/or in vitro binding assays. The results indicate that the association of desmoplakin with desmin depends on sequences within the linker region and C-terminal extremity of desmoplakin, where the B and C subdomains contribute to efficient binding; a potentially phosphorylatable serine residue in the C-terminal extremity of desmoplakin affects its association with desmin; the interaction of desmoplakin with non-filamentous desmin requires sequences contained within the desmin C-terminal rod portion and tail domain in yeast, whereas in in vitro binding studies the desmin tail is dispensable for association; and mutations in either the C-terminus of desmoplakin or the desmin tail linked to inherited cardiomyopathy seem to impair desmoplakindesmin interaction. These studies increase our understanding of desmoplakin-intermediate filament interactions, which are important for maintenance of cytoarchitecture in cardiomyocytes, and give new insights into the molecular basis of desmoplakin- and desmin-related human diseases.

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Section: Resultssupporting

confidence: 82%

Section: Introductionmentioning

confidence: 99%

New insights into the molecular basis of desmoplakinand desmin-related cardiomyopathies

Lapouge

Fontao

Champliaud

et al. 2006

Journal of Cell Science

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show abstract

“…Based on sequence homology and expression, IFs are grouped into six classes, all of which except lamins form predominantly cytoplasmic assemblies (Schweizer et al 2006;Hobbs et al 2016). Here, we focus on epithelial keratins to examine their contribution to the mechanical resilience of epithelia in conjunction with desmosomes, although desmin and vimentin also interact with desmosomes in cardiac tissue, meningiomal, and arachnoidal cells in which they fulfill analogous functions (Kartenbeck et al 1983(Kartenbeck et al , 1984.…”

Section: Role Of Ifs In Mechanical Stability Composition Assembly Amentioning

confidence: 99%

Desmosomes and Intermediate Filaments: Their Consequences for Tissue Mechanics

Hatzfeld

Keil

Magin

2017

Cold Spring Harb Perspect Biol

116

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Adherens junctions (AJs) and desmosomes connect the actin and keratin filament networks of adjacent cells into a mechanical unit. Whereas AJs function in mechanosensing and in transducing mechanical forces between the plasma membrane and the actomyosin cytoskeleton, desmosomes and intermediate filaments (IFs) provide mechanical stability required to maintain tissue architecture and integrity when the tissues are exposed to mechanical stress. Desmosomes are essential for stable intercellular cohesion, whereas keratins determine cell mechanics but are not involved in generating tension. Here, we summarize the current knowledge of the role of IFs and desmosomes in tissue mechanics and discuss whether the desmosome-keratin scaffold might be actively involved in mechanosensing and in the conversion of chemical signals into mechanical strength.

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“…Structurally, desmin has a central ahelical coil rod subdivided into coil 1A, linker 1 (L1), coil 1B, linker 12 (L12) and coil 2, which is flanked by non-helical head and tail domains (Herrmann and Aebi, 2004;Nicolet et al, 2010;Parry et al, 2007). Desmin filaments also have an abundant distribution at the intercalated discs and as a highly interwoven network of desmin filaments extending along myofibers (Georgatos et al, 1987;Kartenbeck et al, 1983;Meng et al, 1997;Nag and Huffaker, 1998;O'Neill et al, 2002;Price, 1984;Tokuyasu et al, 1985;Wang and Ramirez-Mitchell, 1983). …”

Section: Introductionmentioning

confidence: 99%

The desmin coil 1B mutation K190A impairs nebulin Z-disc assembly and destabilizes actin thin filaments

Conover

Gregorio

2011

Journal of Cell Science

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SummaryDesmin intermediate filaments intimately surround myofibrils in vertebrate muscle forming a mesh-like filament network. Desmin attaches to sarcomeres through its high-affinity association with nebulin, a giant F-actin binding protein that co-extends along the length of actin thin filaments. Here, we further investigated the functional significance of the association of desmin and nebulin in cultured primary myocytes to address the hypothesis that this association is key in integrating myofibrils to the intermediate filament network. Surprisingly, we identified eight peptides along the length of desmin that are capable of binding to C-terminal modules 160-170 in nebulin. In this study, we identified a targeted mutation (K190A) in the desmin coil 1B region that results in its reduced binding with the nebulin C-terminal modules. Using immunofluorescence microscopy and quantitative analysis, we demonstrate that expression of the mutant desmin K190A in primary myocytes results in a significant reduction in assembled endogenous nebulin and desmin at the Z-disc. Non-uniform actin filaments were markedly prevalent in myocytes expressing GFP-tagged desmin K190A, suggesting that the nearcrystalline organization of actin filaments in striated muscle depends on a stable interaction between desmin and nebulin. All together, these data are consistent with a model in which Z-disc-associated nebulin interacts with desmin through multiple sites to provide efficient stability to satisfy the dynamic contractile activity of myocytes.

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Specific attachment of desmin filaments to desmosomal plaques in cardiac myocytes.

Cited by 117 publications

References 52 publications

New insights into the molecular basis of desmoplakinand desmin-related cardiomyopathies

New insights into the molecular basis of desmoplakinand desmin-related cardiomyopathies

Desmosomes and Intermediate Filaments: Their Consequences for Tissue Mechanics

The desmin coil 1B mutation K190A impairs nebulin Z-disc assembly and destabilizes actin thin filaments

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