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• W3122990779 abstract "Detyrosination of the α-tubulin C-terminal tail is a post-translational modification (PTM) of microtubules that is key for many biological processes.1Nieuwenhuis J. Brummelkamp T.R. The Tubulin Detyrosination Cycle: Function and Enzymes.Trends Cell Biol. 2019; 29: 80-92Abstract Full Text Full Text PDF PubMed Scopus (41) Google Scholar Although detyrosination is the oldest known microtubule PTM,2Raybin D. Flavin M. An enzyme tyrosylating alpha-tubulin and its role in microtubule assembly.Biochem. Biophys. Res. Commun. 1975; 65: 1088-1095Crossref PubMed Scopus (124) Google Scholar, 3Raybin D. Flavin M. Enzyme which specifically adds tyrosine to the alpha chain of tubulin.Biochemistry. 1977; 16: 2189-2194Crossref PubMed Scopus (141) Google Scholar, 4Raybin D. Flavin M. Modification of tubulin by tyrosylation in cells and extracts and its effect on assembly in vitro.J. Cell Biol. 1977; 73: 492-504Crossref PubMed Scopus (105) Google Scholar, 5Hallak M.E. Rodríguez J.A. Barra H.S. Caputto R. Release of tyrosine from tyrosinated tubulin. Some common factors that affect this process and the assembly of tubulin.FEBS Lett. 1977; 73: 147-150Crossref PubMed Scopus (112) Google Scholar, 6Rodrĭguez J.A. Arce C.A. Barra H.S. Caputto R. Release of tyrosine incorporated as a single unit into rat brain protein.Biochem. Biophys. Res. Commun. 1973; 54: 335-340Crossref PubMed Scopus (31) Google Scholar, 7Barra H.S. Arce C.A. Rodríguez J.A. Caputto R. Some common properties of the protein that incorporates tyrosine as a single unit and the microtubule proteins.Biochem. Biophys. Res. Commun. 1974; 60: 1384-1390Crossref PubMed Scopus (124) Google Scholar the carboxypeptidase responsible for this modification, VASH1/2-SVBP, was identified only 3 years ago,8Nieuwenhuis J. Adamopoulos A. Bleijerveld O.B. Mazouzi A. Stickel E. Celie P. Altelaar M. Knipscheer P. Perrakis A. Blomen V.A. Brummelkamp T.R. Vasohibins encode tubulin detyrosinating activity.Science. 2017; 358: 1453-1456Crossref PubMed Scopus (89) Google Scholar,9Aillaud C. Bosc C. Peris L. Bosson A. Heemeryck P. Van Dijk J. Le Friec J. Boulan B. Vossier F. Sanman L.E. et al.Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation.Science. 2017; 358: 1448-1453Crossref PubMed Scopus (106) Google Scholar precluding genetic approaches to prevent detyrosination. Studies examining the cellular functions of detyrosination have therefore relied on a natural product, parthenolide, which is widely believed to block detyrosination of α-tubulin in cells, presumably by inhibiting the activity of the relevant carboxypeptidase(s).10Freund R.R.A. Gobrecht P. Fischer D. Arndt H.-D. Advances in chemistry and bioactivity of parthenolide.Nat. Prod. Rep. 2020; 37: 541-565Crossref PubMed Google Scholar Parthenolide is a sesquiterpene lactone that forms covalent linkages predominantly with exposed thiol groups; e.g., on cysteine residues.11Ghantous A. Gali-Muhtasib H. Vuorela H. Saliba N.A. Darwiche N. What made sesquiterpene lactones reach cancer clinical trials?.Drug Discov. Today. 2010; 15: 668-678Crossref PubMed Scopus (458) Google Scholar, 12Kreuger M.R.O. Grootjans S. Biavatti M.W. Vandenabeele P. D’Herde K. Sesquiterpene lactones as drugs with multiple targets in cancer treatment: focus on parthenolide.Anticancer Drugs. 2012; 23: 883-896Crossref PubMed Scopus (151) Google Scholar, 13Jackson P.A. Widen J.C. Harki D.A. Brummond K.M. Covalent Modifiers: A Chemical Perspective on the Reactivity of α,β-Unsaturated Carbonyls with Thiols via Hetero-Michael Addition Reactions.J. Med. Chem. 2017; 60: 839-885Crossref PubMed Scopus (244) Google Scholar Using mass spectrometry, we show that parthenolide forms adducts on both cysteine and histidine residues on tubulin itself, in vitro and in cells. Parthenolide causes tubulin protein aggregation and prevents the formation of microtubules. In contrast to epoY, an epoxide inhibitor of VASH1/2-SVBP,9Aillaud C. Bosc C. Peris L. Bosson A. Heemeryck P. Van Dijk J. Le Friec J. Boulan B. Vossier F. Sanman L.E. et al.Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation.Science. 2017; 358: 1448-1453Crossref PubMed Scopus (106) Google Scholar parthenolide does not block VASH1-SVBP activity in vitro. Lastly, we show that epoY is an efficacious inhibitor of microtubule detyrosination in cells, providing an alternative chemical means to block detyrosination. Collectively, our work supports the notion that parthenolide is a promiscuous inhibitor of many cellular processes and suggests that its ability to block detyrosination may be an indirect consequence of reducing the polymerization-competent pool of tubulin in cells." @default.
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• W3122990779 date "2021-02-01" @default.
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• W3122990779 title "Parthenolide Destabilizes Microtubules by Covalently Modifying Tubulin" @default.
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• W3122990779 doi "https://doi.org/10.1016/j.cub.2020.11.055" @default.
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