ArticlePloS one2011
Dysferlin interacts with histone deacetylase 6 and increases alpha-tubulin acetylation.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. It is linked to trial NCT01863004 (Proteasomal Inhibition for Patients With Mis-sense Mutated Dysferlin), which is not on this map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Proteasomal Inhibition for Patients With Mis-sense Mutated Dysferlin
Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Proteins implicated in muscular dystrophy and cancer are functional constituents of the centrosome.Life science alliance · 2022Article
- Review
- G protein-coupled receptor kinase 5 modifies cancer cell resistance to paclitaxel.Molecular and cellular biochemistry · 2019Article
- Faster regeneration associated to high expression of Fam65b and Hdac6 in dysferlin-deficient mouse.Journal of molecular histology · 2019Article
- Retraction: Dysferlin Interacts with Histone Deacetylase 6 and Increases alpha-Tubulin Acetylation.PloS one · 2018Article
- Emerging Functional Differences between the Synaptotagmin and Ferlin Calcium Sensor Families.Biochemistry · 2017Article
- Inhibition of HDAC6 activity through interaction with RanBPM and its associated CTLH complex.BMC cancer · 2017Article
- EWSR1 regulates mitosis by dynamically influencing microtubule acetylation.Cell cycle (Georgetown, Tex.) · 2016Article
- Exploration of the labeling of [11C]tubastatin A at the hydroxamic acid site with [11C]carbon monoxide.Journal of labelled compounds & radiopharmaceuticals · 2016Article
- Promiscuous actions of small molecule inhibitors of the protein kinase D-class IIa HDAC axis in striated muscle.FEBS letters · 2015Article
- HDAC6 contributes to pathological responses of heart and skeletal muscle to chronic angiotensin-II signaling.American journal of physiology. Heart and circulatory physiology · 2014Article
- Fam65b is important for formation of the HDAC6-dysferlin protein complex during myogenic cell differentiation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Dysferlin is essential for endocytosis in the sea star oocyte.Developmental biology · 2014Article
- Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure.Molecular biology of the cell · 2014Article
- Dysferlin at transverse tubules regulates Ca(2+) homeostasis in skeletal muscle.Frontiers in physiology · 2014Review
- Genetic silencing of Nrf2 enhances X-ROS in dysferlin-deficient muscle.Frontiers in physiology · 2014Article
- Dysferlin stabilizes stress-induced Ca2+ signaling in the transverse tubule membrane.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- HDAC6 and ovarian cancer.International journal of molecular sciences · 2013Review
- Article
- Modular dispensability of dysferlin C2 domains reveals rational design for mini-dysferlin molecules.The Journal of biological chemistry · 2012Article
Corrections and comments
- Retraction · 2018-01-29Falsification/Fabrication of Data · Falsification/Fabrication of Image · Investigation by Company/Institution ·
- Retracted
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
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.
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Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.