Des Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
Desmin
| Protein Name | DES (Desmin) |
|---|---|
| Gene | DES |
| UniProt ID | P17661 |
| PDB ID | 1K40, 3T7G |
| Molecular Weight | 53 kDa |
| Subcellular Localization | Cytoplasm, intermediate filaments |
| Protein Family | Type III intermediate filament family |
DES PROTEIN is a gene/protein encoding a key neuronal protein involved in synaptic function, signal transduction, and cellular homeostasis. Dysfunction of DES PROTEIN is associated with neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, and related disorders.
Desmin is a type III intermediate filament protein with an N-terminal non-helical head domain (approximately 85 residues), a central alpha-helical rod domain (approximately 310 residues organized into 1A, 1B, 2A, and 2B segments), and a C-terminal non-helical tail domain (approximately 100 residues) [1]. The rod domain contains heptad repeats that drive coiled-coil formation essential for filament assembly [2].
Desmin functions as the primary intermediate filament in mature skeletal and cardiac muscle, providing structural integrity to the sarcomere Z-disk and connects the contractile apparatus to the nucleus, mitochondria, and other organelles [3]. Key functions include:
While primarily a muscle-specific protein, desmin pathology has been observed in certain neurodegenerative conditions:
Pathogenic mechanisms include protein aggregate formation, disrupted Z-disk structure, and muscle fiber degeneration [4]. Mutations in DES gene cause autosomal dominant myofibrillar myopathy with characteristic desmin-positive inclusions.
Desmin mutations cause cardiac muscle weakness and heart failure, often with conduction system disease [5].
Rare DES mutations have been associated with Charcot-Marie-Tooth disease type 2 (CMT2) phenotypes [6].
The study of Des Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
Last updated: 2026-03-05
Herrmann H, Aebi U. Intermediate filaments: structure and assembly. Cold Spring Harb Perspect Biol. 2010;2(12):a000620. PMID:21088442 ↩︎
Strelkov SV, et al. Crystal structure of the central alpha-helical domain of desmin. J Mol Biol. 2002;323(4):665-683. PMID:12419257 ↩︎
Capetanaki Y, et al. Desmin in muscle formation and maintenance: knockouts and consequences. Cell Struct Funct. 2007;32(1):17-26. PMID:17519548 ↩︎
Schröder R, Schoser B. Myofibrillar myopathies: a clinical and morphopathological approach. Brain. 2009;132(Pt 8):2003-2018. PMID:19414478 ↩︎
Dalakas MC, et al. Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by mutations in the desmin gene. N Engl J Med. 2000;342(11):770-780. PMID:10717011 ↩︎
Jacquemont S, et al. Charcot-Marie-Tooth disease type 2 and desmin-related myopathy. Neurology. 2001;57(10):1881-1885. PMID:11723286 ↩︎