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2020, doi:10.1016/j.bbamcr.2020.118788. It maintains the structural and functional integrity of the myofibrils and functions as a cytoskeletal protein linking Z bands to the plasma membrane. The inheritance pattern is usually autosomal dominant; however, sporadic mutations also occur [40]. Thus, the loss of N-terminal fragment of desmin molecule disrupts its binding to mitochondria. Mice overexpressing mutant R120G-αB-crystallin displayed a phenotype with striking similarity to desminopathy in humans. Colan, in Cardioskeletal Myopathies in Children and Young Adults, 2017. Since leupeptin and E-64 are known to inhibit cysteine proteases, in contrast to serine protease inhibitors PMSF, aprotinin, and TAME, we inferred that a candidate belongs to the cysteine proteases. Recently, abnormal cytoplasmic reactivity for caveolin-3 and aggregates of vesicular and tubular structures were shown in a patient with desminopathy (Shinde et al., 2008). [PMC free article] Geisler N, Weber K. Phosphorylation of desmin in vitro inhibits formation of intermediate filaments; identification of three kinase A sites in the aminoterminal head domain. Desmin is a specific marker for myogenic differentiation among soft tissue tumors, seen in almost all rhabdomyosarcomas/leiomyosarcomas, rhabdomyomas/leiomyomas. This form of RCM may be associated with skeletal myopathy and/or conduction system disease. 2015, 29, 820–827. Desmin accumulation in skeletal and cardiac muscle has been observed in the absence of DES gene mutations and it remains uncertain whether under these circumstances it represents a nonspecific finding. ; Minin, A.A. Mitochondrial membrane potential is regulated by vimentin intermediate filaments. Like other intermediate filaments, desmin displays a 20 to 22 nm axial periodicity. These data suggest that interaction with desmin is a prerequisite for normal mitochondrial functioning. Siklos, M.; BenAissa, M.; Thatcher, G.R. ; Goldman, R.D. Calpain 10: A mitochondrial calpain and its role in calcium-induced mitochondrial dysfunction. Protoc. ; et al. The protein can be extensively modified posttranslationally (http://www.phosphosite.org/) and particular attention has been focused on phosphorylation at multiple residues (between 17 and 40) and the role that posttranslational modification might play in filament assembly [75], myofibrillar disarray [73], and cardiovascular pathology in general [1,180]. Mol. ; Minin, A.A. Vimentin intermediate filaments modulate the motility of mitochondria. Although desmin is most often expressed by myogenous cells, in vitro studies of chicken embryo and hamster kidney fibroblasts have also revealed its presence.34 This finding is best explained by implicating a myofibroblastic nature for such cells. The RCM phenotype has not been reported in children with Emery–Dreifuss to date. In human heart failure, desmin expression is upregulated, which has been hypothesized to be a defense mechanism in an attempt to maintain normal sarcomere alignment amidst disease pathogenesis. ; Kuczmarski, E.R. [12] The tail domain is responsible for the integration of filaments and interaction with proteins and organelles. PCD, precoiled-coil domain. Desmin and vimentin are the main components of intermediate filaments implicated in mechanotransduction (Figure 2.1). However, incubation in the absence of inhibitor led to its shortening and to the loss of the ability to co-sediment with mitochondria (Figure 5, lines S2 and P2). The cytoplasmic actins, while distributed throughout the cell, are clustered in bundles and networks near the cell surface where they attach to the sarcolemma via discrete interacting proteins, including those that constitute the costameres (not shown). Muscle atrophy, mild facial weakness, dysphagia, dysarthria, and respiratory insufficiency can occur. [37] In addition, DES mutations cause frequently cardiac conduction diseases. Using desmin mutant Des(Y122L) that forms unit-length filaments (ULFs) but is incapable of forming long filaments and, therefore, could be effectively separated from mitochondria by centrifugation through sucrose gradient, we probed the interaction of recombinant human desmin with mitochondria isolated from rat liver. Non-cleaved desmin is seen both in supernatant and pellet only when calpeptin was added (S1, P1). [39], GRCh38: Ensembl release 89: ENSG00000175084, GRCm38: Ensembl release 89: ENSMUSG00000026208, "A dysfunctional desmin mutation in a patient with severe generalized myopathy", "Molecular insights into cardiomyopathies associated with desmin (DES) mutations", "The physiological role of cardiac cytoskeleton and its alterations in heart failure", "Mass spectrometry characterization of human DES at COPaKB", "Integration of cardiac proteome biology and medicine by a specialized knowledgebase", "Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle", "Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments", "Alpha B-crystallin in cardiac tissue. The lysates are sonicated, centrifuged as above, and dialyzed against dialysis buffer 1 (1 M urea, 10 mM Tris–HCl pH 8, 5 mM EDTA, 20 mM NaCl, 0.1% NP-40, 0.1% DOC, 5% glycerol, protease inhibitor cocktail, 2 mM phenylmethylsulfonylfluoride) overnight at 4 °C and dialysis buffer 2 (dialysis buffer 1 without urea) for 8–10 h at 4 °C. Genetic analysis of the proband revealed a mutation in the gene encoding lamin A/C (LMNA), initially considered to be the cause of both cases. Previously, we hypothesized [6] that, similarly to vimentin, an N-terminal part of desmin molecule could contain a targeting signal which localizes desmin to the outer mitochondrial membrane (OMM). [34] Some of these DES mutations cause an aggregation of desmin within the cytoplasm. The head domain 84 amino acids with many arginine, serine, and aromatic residues is important in filament assembly and dimer-dimer interactions. Figure 2. Biol. 2020, 182, 636–647. [13] Since desmin is expressed at a low level during differentiation another protein may be able to compensate for desmin's function early in development but not later on. It has a molecular weight of 53 kD. [38], Desmin has been evaluated for role in assessing the depth of invasion of urothelial carcinoma in TURBT specimens. Our data (Figures 2–4) show that the main product of desmin degradation resulting from the incubation with mitochondria was smaller than the initial polypeptide by approximately 10 kD. The sepharose-bound proteins can be used directly for GST pull-down assay. The serum CK level is normal or mildly raised. However, it can also be an autosomal disorder caused by mutations in the gene encoding for lamin A and lamin C (LMNA) on chromosome 1q21.2-q21.3 [38]. The scapuloperoneal syndrome of Kaeser has now been traced to an autosomal dominant mutation in desmin in a large kinship (Walter et al., 2007). A similar protein, vimentin, is present in higher amounts during embryogenesis while desmin is present in higher amounts after differentiation. Desmin is encoded by a single gene, DES, located at 2q35.

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