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Updated: May 7, 2026

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
Published on: May 18, 2017
Posttranslational modifications of desmin and their implication in biological processes and pathologies
Daniel L Winter1, Denise Paulin, Mathias Mericskay
1Department of Aging, Stress and Inflammation, Université Pierre et Marie Curie (Univ Paris 6), Sorbonne Universités, Paris, France, daniel.winter@pasteur.fr.
Posttranslational modifications (PTMs) regulate desmin filaments, crucial for muscle structure and function. Understanding these desmin PTMs offers insights into muscle diseases and potential therapeutic strategies.
Area of Science:
- Muscle biology
- Cellular structure
- Biochemistry
Background:
- Desmin is a muscle-specific intermediate filament protein.
- Desmin is implicated in myofibrillar myopathies, dilated cardiomyopathy, and muscle wasting.
- Desmin undergoes various posttranslational modifications (PTMs) and nonenzymatic modifications.
Purpose of the Study:
- To review findings on desmin PTMs and their roles in biological processes and pathologies.
- To discuss the regulation of the desmin network by PTMs.
- To highlight the potential of advanced tools for studying desminopathies.
Main Methods:
- Literature review of studies on desmin PTMs.
- Analysis of identified PTM target residues and modifying enzymes.
- Discussion of the functional consequences of desmin modifications.
Main Results:
- Phosphorylation and ADP-ribosylation of desmin lead to filament disassembly.
- Ubiquitylation targets desmin for degradation.
- Desmin PTMs are involved in myogenesis, muscle contraction, atrophy, and cell division.
Conclusions:
- The desmin filament network acts as a scaffold regulated by PTMs, impacting muscle cell structure and function.
- PTMs play a critical role in desmin-related myopathies (desminopathies).
- Further research utilizing advanced imaging and PTM analysis tools is recommended for desminopathies.
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