Dysferlin Interacts with Histone Deacetylase 6 and Increases alpha-Tubulin Acetylation
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Dossier post-publication
- Nature
- Retraction
- Motif
- Falsification/Fabrication of Data;Falsification/Fabrication of Image;Investigation by Company/Institution;
- Date
- 1/29/2018 0:00
- Signalé par OpenAlex ?
- Oui
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Résumé
Dysferlin is a multi-C2 domain transmembrane protein involved in a plethora of cellular functions, most notably in skeletal muscle membrane repair, but also in myogenesis, cellular adhesion and intercellular calcium signaling. We previously showed that dysferlin interacts with alpha-tubulin and microtubules in muscle cells. Microtubules are heavily reorganized during myogenesis to sustain growth and elongation of the nascent muscle fiber. Microtubule function is regulated by post-translational modifications, such as acetylation of its alpha-tubulin subunit, which is modulated by the histone deacetylase 6 (HDAC6) enzyme. In this study, we identified HDAC6 as a novel dysferlin-binding partner. Dysferlin prevents HDAC6 from deacetylating alpha-tubulin by physically binding to both the enzyme, via its C2D domain, and to the substrate, alpha-tubulin, via its C2A and C2B domains. We further show that dysferlin expression promotes alpha-tubulin acetylation, as well as increased microtubule resistance to, and recovery from, Nocodazole- and cold-induced depolymerization. By selectively inhibiting HDAC6 using Tubastatin A, we demonstrate that myotube formation was impaired when alpha-tubulin was hyperacetylated early in the myogenic process; however, myotube elongation occurred when alpha-tubulin was hyperacetylated in myotubes. This study suggests a novel role for dysferlin in myogenesis and identifies HDAC6 as a novel dysferlin-interacting protein.
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La notice
- Revue
- PLoS ONE
- Thématique
- Histone Deacetylase Inhibitors Research
- Domaine
- Biochemistry, Genetics and Molecular Biology
- Établissements canadiens
- McGill UniversityMontreal Neurological Institute and Hospital
- Organismes subventionnaires
- Canadian Institutes of Health ResearchBundesministerium für Bildung und ForschungSchweizerischer Nationalfonds zur Förderung der Wissenschaftlichen ForschungNational Science Foundation
- Mots-clés
- MyogenesisCell biologyDysferlinTubulinAcetylationBiologyMicrotubuleTransmembrane proteinHDAC6NocodazoleHistone deacetylaseChemistryMyocyteHistoneBiochemistryCytoskeletonSkeletal muscleCellReceptorAnatomy
- Résumé présent dans OpenAlex
- oui