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Syncoilin is an atypical type III intermediate filament (IF) protein, which is expressed in muscle and is associated with the dystrophin-associated protein complex. Here, we show that syncoilin is expressed in both the central and peripheral nervous systems. Isoform Sync1 is dominant in the brain, but isoform Sync2 is dominant in the spinal cord and sciatic nerve. Peripherin is a type III IF protein that has been shown to colocalise and interact with syncoilin. Our analyses suggest that syncoilin might function to modulate formation of peripherin filament networks through binding to peripherin isoforms. Peripherin is associated with the disease amyotrophic lateral sclerosis (ALS), thus establishing a link between syncoilin and ALS. A neuronal analysis of the syncoilin-null mouse (Sync(-/-)) revealed a reduced ability in accelerating treadmill and rotarod tests. This phenotype might be attributable to the impaired function of extensor digitorum longus muscle and type IIb fibres caused by a shift from large- to small-calibre motor axons in the ventral root.

Original publication




Journal article


J Cell Sci

Publication Date





2543 - 2552


Amyotrophic Lateral Sclerosis, Animals, Brain, Cell Line, Tumor, Fluorescent Antibody Technique, Humans, Immunoblotting, Immunoprecipitation, Intermediate Filament Proteins, Membrane Glycoproteins, Mice, Mice, Knockout, Motor Neurons, Muscle Proteins, Nerve Tissue Proteins, Peripherins, Polymerase Chain Reaction, Protein Binding, Protein Isoforms, Sciatic Nerve, Spinal Cord