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Dynein mutations associated with hereditary motor neuropathies impair mitochondrial morphology and function with age
Journal article   Peer reviewed

Dynein mutations associated with hereditary motor neuropathies impair mitochondrial morphology and function with age

Judith Eschbach, Jérôme Sinniger, Jamal Bouitbir, Anissa Fergani, Anna-Isabel Schlagowski, Joffrey Zoll, Bernard Geny, Frédérique René, Yves Larmet, Vincent Marion, …
Neurobiology of disease, Vol.58, pp.220-230
10/2013
DOI: 10.1016/j.nbd.2013.05.015
PMID: 23742762
url
https://doaj.org/article/7d3226828a914e8f87d56033c9cb35bfView
Open Access

Abstract

Mutations in the DYNC1H1 gene encoding for dynein heavy chain cause two closely related human motor neuropathies, dominant spinal muscular atrophy with lower extremity predominance (SMA–LED) and axonal Charcot–Marie–Tooth (CMT) disease, and lead to sensory neuropathy and striatal atrophy in mutant mice. Dynein is the molecular motor carrying mitochondria retrogradely on microtubules, yet the consequences of dynein mutations on mitochondrial physiology have not been explored. Here, we show that mouse fibroblasts bearing heterozygous or homozygous point mutation in Dync1h1, similar to human mutations, show profoundly abnormal mitochondrial morphology associated with the loss of mitofusin 1. Furthermore, heterozygous Dync1h1 mutant mice display progressive mitochondrial dysfunction in muscle and mitochondria progressively increase in size and invade sarcomeres. As a likely consequence of systemic mitochondrial dysfunction, Dync1h1 mutant mice develop hyperinsulinemia and hyperglycemia and progress to glucose intolerance with age. Similar defects in mitochondrial morphology and mitofusin levels are observed in fibroblasts from patients with SMA–LED. Last, we show that Dync1h1 mutant fibroblasts show impaired perinuclear clustering of mitochondria in response to mitochondrial uncoupling. Our results show that dynein function is required for the maintenance of mitochondrial morphology and function with aging and suggest that mitochondrial dysfunction contributes to dynein-dependent neurological diseases, such as SMA–LED. [Display omitted] •Human and murine dynein mutations lead to mitochondrial fragmentation in cultured fibroblasts.•Human and murine dynein mutant fibroblasts display decreased levels of mitofusin 1.•Murine dynein mutant fibroblasts display impaired mitochondrial clustering in response to mitochondrial uncoupling.•Mouse Cramping dynein mutation leads to widespread mitochondrial dysfunction and glucose intolerance in vivo.
Charcot–Marie–Tooth disease Mitochondria Diabetes Dynein Motor neuron disease Spinal muscular atrophy

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