Language

English

Publication Date

3-1-2024

Journal

The Journal of Physiology

DOI

10.1113/JP285894

PMID

38441922

PMCID

PMC10942750

PubMedCentral® Posted Date

3-5-2025

PubMedCentral® Full Text Version

Author MSS

Abstract

Spectrins function together with actin as obligatory subunits of the submembranous cytoskeleton. Spectrins maintain cell shape, resist mechanical forces, and stabilize ion channel and transporter protein complexes through binding to scaffolding proteins. Recently, pathogenic variants of SPTBN4 (β4 spectrin) were reported to cause both neuropathy and myopathy. Although β4 spectrin's role in neurons is mostly understood, its function in skeletal muscle, another excitable tissue subject to large forces, is unknown. Here, using a muscle specific β4 spectrin conditional knockout mouse, we show that β4 spectrin does not contribute to muscle function. In addition, we show β4 spectrin is not present in muscle, indicating the previously reported myopathy associated with pathogenic SPTBN4 variants is neurogenic in origin. More broadly, we show that α2, β1, and β2 spectrins are found in skeletal muscle, with α2 and β1 spectrins being enriched at the postsynaptic neuromuscular junction (NMJ). Surprisingly, using muscle specific conditional knockout mice, we show that loss of α2 and β2 spectrins had no effect on muscle health, function, or the enrichment of β1 spectrin at the NMJ. Muscle specific deletion of β1 spectrin also had no effect on muscle health, but with increasing age resulted in the loss of clustered NMJ Na+ channels. Together our results suggest that muscle β1 spectrin functions independently of an associated α spectrin to maintain Na+ channel clustering at the postsynaptic NMJ. Furthermore, despite repeated exposure to strong forces and in contrast to neurons, muscles do not require spectrin cytoskeletons to maintain cell shape or integrity.

Keywords

Animals, Humans, Mice, Actin Cytoskeleton, Muscle, Skeletal, Muscular Diseases, Neuromuscular Junction, Spectrin, Sodium Channels, cytoskeleton, regeneration, neuromuscular junction, repair, axon injury

Published Open-Access

yes

nihms-1968521-f0001.jpg (228 kB)
Graphical Abstract

Included in

Neurosciences Commons

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