ArticleTurkish journal of biology = Turk biyoloji dergisi2026
Modulating microtubule stability via α-tubulin acetylation partially restores Golgi fragmentation in spinal muscular atrophy.
Article in Turkish journal of biology = Turk biyoloji dergisi, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Background/aim: Spinal muscular atrophy (SMA) is a neurodegenerative disease caused by the loss of survival of motor neuron (SMN) protein. SMN deficiency leads to perturbations of the cytoskeleton, including microtubules, which are mainly involved in motility-related cellular processes. However, the molecular mechanisms of microtubule dysregulation in SMA remain elusive. Alpha (α)-tubulin is a structural component of microtubules, and its posttranslational modifications affect microtubule dynamics. Here, we aimed to investigate α-tubulin acetylation and related molecular mechanisms in SMA. Materials and methods: Two different SMA mouse models, the Results: The acetylation level of α-tubulin was decreased in the Conclusion: Our findings provide new insight into the molecular basis of SMA, indicating that cellular pathologies, including abnormal Golgi morphology, are associated with microtubule dysregulations caused by altered α-tubulin posttranslational modifications and regulatory proteins. Our findings support that microtubule perturbations are part of SMA pathology.
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