MINI REVIEW article
Front. Mol. Neurosci.
Sec. Brain Disease Mechanisms
This article is part of the Research TopicEmerging Mechanisms in Neurodegenerative Disease Pathogenesis: Vertebrate and Invertebrate Model OrganismsView all 3 articles
Potential role of stress granules and myogranules in amyotrophic lateral sclerosis
Provisionally accepted
- Institute for Physical Activity and Nutrition, School of Exercise and Nutrition Sciences, Deakin University, Geelong, Australia
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Amyotrophic lateral sclerosis (ALS) is characterized by the progressive loss of upper and lower motor neurones, leading to muscle wasting, paralysis and respiratory failure. Pathological cytoplasmic aggregation of the RNA-binding protein transactive response DNA-binding protein 43 (TDP-43) protein occurs in neural tissues in ~97% of all ALS cases, and is also observed in skeletal muscle. Cytoplasmic aggregation of TDP-43 is believed to contribute to ALS pathogenesis; however, its precise mechanistic role/s continues to elude the field. This mini review explores the potential role and regulation of two TDP-43-associated RNA-protein assemblies, stress granules (SGs) and myogranules (MGs). We review the current understanding of SG and MG formation and their potential role in ALS-related neurodegeneration and muscle pathology. We also highlight limitations and strengths and suggest future directions for research.
Keywords: Amyotrophic Lateral Sclerosis, Brain, myogranule, Skeletalmuscle, Spinal Cord, stress granules, TDP-43
Received: 15 Aug 2025; Accepted: 11 Dec 2025.
Copyright: © 2025 Ishaq and Russell. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Saddam Muhammad Ishaq
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