{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lopes D"],"funding":["Fundação para a Ciência e a Tecnologia","European Research Council","European Union’s Horizon 2020","La Caixa Health Research","European Regional Development Fund"],"pagination":["e202205092"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9723805"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["222(2)"],"pubmed_abstract":["α/β-Tubulin posttranslational modifications (PTMs) generate microtubule diversity, but whether they account for cancer cell resistance to microtubule-targeting drugs remains unknown. Here, we performed a pilot dissection of the \"cancer tubulin code\" using the NCI-60 cancer cell panel. We found that acetylated, detyrosinated, and ∆2-α-tubulin that typically accumulate on stable microtubules were uncoupled in many cancer cells. Acetylated α-tubulin did not affect microtubule dynamics, whereas its levels correlated with, but were not required for, taxol-induced cytotoxicity. In contrast, experimental increase of α-tubulin detyrosination, and/or depletion of the detyrosination-sensitive microtubule-depolymerizing enzyme MCAK, enhanced taxol-induced cytotoxicity by promoting cell death in mitos"],"journal":["The Journal of cell biology"],"pubmed_title":["α-Tubulin detyrosination links the suppression of MCAK activity with taxol cytotoxicity."],"pmcid":["PMC9723805"],"funding_grant_id":["/135077/2017","PTDC/MED-","SFRH/","681443","/3479/2020","NORTE-01-0145-FEDER-000051","/PR/HR21/52410025"],"pubmed_authors":["Lopes D","Seabra AL","Maiato H","Orr B"],"additional_accession":[]},"is_claimable":false,"name":"α-Tubulin detyrosination links the suppression of MCAK activity with taxol cytotoxicity.","description":"α/β-Tubulin posttranslational modifications (PTMs) generate microtubule diversity, but whether they account for cancer cell resistance to microtubule-targeting drugs remains unknown. Here, we performed a pilot dissection of the \"cancer tubulin code\" using the NCI-60 cancer cell panel. We found that acetylated, detyrosinated, and ∆2-α-tubulin that typically accumulate on stable microtubules were uncoupled in many cancer cells. Acetylated α-tubulin did not affect microtubule dynamics, whereas its levels correlated with, but were not required for, taxol-induced cytotoxicity. In contrast, experimental increase of α-tubulin detyrosination, and/or depletion of the detyrosination-sensitive microtubule-depolymerizing enzyme MCAK, enhanced taxol-induced cytotoxicity by promoting cell death in mitos","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2025-04-19T04:20:27.056Z","creation":"2025-04-19T04:20:27.056Z"},"accession":"S-EPMC9723805","cross_references":{"pubmed":["36459065"],"doi":["10.1083/jcb.202205092"]}}