ArticleThe Journal of biological chemistry2015
Tubulin tail sequences and post-translational modifications regulate closure of mitochondrial voltage-dependent anion channel (VDAC).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- Role of tubulin post-translational modifications in peripheral neuropathy.Experimental neurology · 2023Review
- Biomimetic Polyphosphate Materials: Toward Application in Regenerative Medicine.Progress in molecular and subcellular biology · 2022Article
- Loss of RARRES1 function Promotes Follicular Lymphomagenesis and Inhibits B cell Differentiation in Mice.International journal of biological sciences · 2022Article
- Impact of the 'tubulin economy' on the formation and function of the microtubule cytoskeleton.Current opinion in cell biology · 2021Review
- Pathogenic role of delta 2 tubulin in bortezomib-induced peripheral neuropathy.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- Redox Signaling from Mitochondria: Signal Propagation and Its Targets.Biomolecules · 2020Review
- Article
- Inorganic Polyphosphates As Storage for and Generator of Metabolic Energy in the Extracellular Matrix.Chemical reviews · 2019Review
- Cardiac microtubules in health and heart disease.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- Tubulin mRNA stability is sensitive to change in microtubule dynamics caused by multiple physiological and toxic cues.PLoS biology · 2019Article
- Tubulin βII and βIII Isoforms as the Regulators of VDAC Channel Permeability in Health and Disease.Cells · 2019Review
- Tumor suppressor RARRES1 links tubulin deglutamylation to mitochondrial metabolism and cell survival.Oncotarget · 2019Article
- Sphingolipids and lipid rafts: Novel concepts and methods of analysis.Chemistry and physics of lipids · 2018Review
- Sequence diversity of tubulin isotypes in regulation of the mitochondrial voltage-dependent anion channel.The Journal of biological chemistry · 2018Article
- A new insight into diffusional escape from a biased cylindrical trap.The Journal of chemical physics · 2017Article
- An Emerging Role for Tubulin Isotypes in Modulating Cancer Biology and Chemotherapy Resistance.International journal of molecular sciences · 2017Review
- Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Association of VDAC with Cell Viability of PC12 Model of Huntington's Disease.Frontiers in oncology · 2016Article
- Katanin Severing and Binding Microtubules Are Inhibited by Tubulin Carboxy Tails.Biophysical journal · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
It was previously shown that tubulin dimer interaction with the mitochondrial outer membrane protein voltage-dependent anion channel (VDAC) blocks traffic through the channel and reduces oxidative metabolism and that this requires the unstructured anionic C-terminal tail peptides found on both α- and β-tubulin subunits. It was unclear whether the α- and β-tubulin tails contribute equally to VDAC blockade and what effects might be due to sequence variations in these tail peptides or to tubulin post-translational modifications, which mostly occur on the tails. The nature of the contribution of the tubulin body beyond acting as an anchor for the tails had not been clarified either. Here we present peptide-protein chimeras to address these questions. These constructs allow us to easily combine a tail peptide with different proteins or combine different tail peptides with a particular protein. The results show that a single tail grafted to an inert protein is sufficient to produce channel closure similar to that observed with tubulin. We show that the β-tail is more than an order of magnitude more potent than the α-tail and that the lower α-tail activity is largely due to the presence of a terminal tyrosine. Detyrosination activates the α-tail, and activation is reversed by the removal of the glutamic acid penultimate to the tyrosine. Nitration of tyrosine reverses the tyrosine inhibition of binding and even induces prolonged VDAC closures. Our results demonstrate that small changes in sequence or post-translational modification of the unstructured tails of tubulin result in substantial changes in VDAC closure.
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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.