Physical evidence on <scp>desmin–lamin</scp> B interaction

Objectives Nucleocytoplasmic transport is one of the key features in regulation of cellular physiology. Developing a better understanding of the molecular mechanism underlying the nucleocytoplasmic shuttling of proteins can broaden our perspective and understanding on the elaborate sorting mechanisms within cells. Desmin is a muscle specific intermediate filament with amphiphilic properties and has interactions with the components of the nuclear pore complex which facilitates the transport between the cytoplasm and nucleus. The study aims to develop a better understanding of the amphiphilic nature of desmin and its relation to nucleocytoplasmic transport. Methods We conducted a proteomic analysis of desmin-immunoprecipitates to identify the nuclear partners of desmin. Additionally, we analysed the amphiphilic nature of desmin using a hydrophobicity assay to determine if it can undergo conformational changes to adapt to a hydrophobic environment. Results Using proteomic and in silico analysis we demonstrated that desmin interacts with several nups. The hydrophobicity assay results showed that desmin can increase its surface hydrophobicity in a hydrophobic environment. Conclusions Our findings suggest that desmin has the ability to undergo conformational changes under favourable conditions and possibly can be transported through nucleus via direct interaction with nups. Further analysis is required to understand the functional implications of this conformational change in vivo. Data are available via ProteomeXchange with identifier PXD047121.

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Assessment of myogenic potency in patient-derived fibroblasts with c.1289-2A>G Desmin mutation

Düz,

Ünsal,

Eerdem-Özdamar

et al. 2024

Turkish Journal of Biochemistry

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Objectives The ultra-rare DES c.1289-2A>G mutation, resulting in a 48-base pair insertion in the Desmin tail domain, is associated with late-onset MFM1 (myofibrillar myopathy-1; OMIM number; 601419) and exhibits distinctive pathological features. Despite sustained expression and cytoskeletal integrity, muscle biopsies reveal dystrophic characteristics through an unidentified mechanism. A deeper understanding of the molecular mechanisms underlying Desmin-related MFM1 could enhance our perspective and comprehension of the disease’s pathophysiology. In this study, we aimed to investigate the pathological phenotype by assessing the myogenic potency of MyoD-induced patient-derived fibroblasts. Methods Following the immortalization and myoconversion of unaffected and patient-derived fibroblast cells, we analyzed the myogenic potency of the mutant and control groups on day 5 post-differentiation. This analysis involved staining cells with MF20 antibody and DAPI after MyoD induction. Results Employing six parameters to quantify extra nuclei and myotube properties, we unveil impaired myogenic differentiation in c.1289-2A>G mutant cells, as evidenced by a compromised fusion index and distinctive myogenic features. In summary, our preliminary findings indicate phenotypic abnormalities and suggest an association between the DES c.1289-2A>G mutation and delayed maturation and MFM in affected individuals. Conclusions Our results indicate a significant involvement of Desmin in the myogenic maturation of muscle cells. Further investigation is required to understand the changes in the transcriptome during the myoconversion of patient-derived fibroblasts.

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Physical evidence on desmin–lamin B interaction

Cited by 3 publications

References 29 publications

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LMNB1 deletion in ovarian cancer inhibits the proliferation and metastasis of tumor cells through PI3K/Akt pathway

Desmin’s conformational modulation by hydrophobicity

Assessment of myogenic potency in patient-derived fibroblasts with c.1289-2A>G Desmin mutation

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