Dysferlin Interacts with Histone Deacetylase 6 and Increases alpha-Tubulin Acetylation
Why is this work in the frame?
A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.
Post-publication record
- Nature
- Retraction
- Reason
- Falsification/Fabrication of Data;Falsification/Fabrication of Image;Investigation by Company/Institution;
- Date
- 1/29/2018 0:00
- Flagged by OpenAlex?
- Yes
Source: Retraction Watch, joined by DOI. OpenAlex records retraction as is_retracted, a boolean over a state space with at least four values, so it cannot express an expression of concern, a correction or a reinstatement — it reports them as false, which reads as “fine”.
Abstract
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.
Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.
The record
- Venue
- PLoS ONE
- Topic
- Histone Deacetylase Inhibitors Research
- Field
- Biochemistry, Genetics and Molecular Biology
- Canadian institutions
- McGill UniversityMontreal Neurological Institute and Hospital
- Funders
- Canadian Institutes of Health ResearchBundesministerium für Bildung und ForschungSchweizerischer Nationalfonds zur Förderung der Wissenschaftlichen ForschungNational Science Foundation
- Keywords
- MyogenesisCell biologyDysferlinTubulinAcetylationBiologyMicrotubuleTransmembrane proteinHDAC6NocodazoleHistone deacetylaseChemistryMyocyteHistoneBiochemistryCytoskeletonSkeletal muscleCellReceptorAnatomy
- Has abstract in OpenAlex
- yes