{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T06:36:20Z","timestamp":1787812580553,"version":"build-2784847793"},"reference-count":58,"publisher":"Shared Science Publishers OG","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"Abstract<\/jats:title>\n \n Post-translational modifications of microtubules regulate their stability and dynamics. Acetylation of\n \n \n \u03b1<\/mml:mi>\n <\/mml:math>\n <\/jats:inline-formula>\n tubulin at lysine 40 (K40) by\n \n \n \u03b1<\/mml:mi>\n <\/mml:math>\n <\/jats:inline-formula>\n -acetyltransferase (\n \n \n \u03b1<\/mml:mi>\n <\/mml:math>\n <\/jats:inline-formula>\n TAT) occurs on the luminal side of microtubules, stabilizes their structure, and plays essential roles in various cellular processes across eukaryotes. Apicomplexan parasites include the malaria-causing\n Plasmodium<\/jats:italic>\n species and\n Toxoplasma gondii<\/jats:italic>\n , both of which possess unusually stable subpellicular microtubules, a set of cytoskeletal filaments underlying the parasite\u2019s inner membrane complex. Interestingly, while\n Toxoplasma gondii<\/jats:italic>\n and human-infecting\n Plasmodium<\/jats:italic>\n species retain both K40 and\n \n \n \u03b1<\/mml:mi>\n <\/mml:math>\n <\/jats:inline-formula>\n TAT, rodent-infecting\n Plasmodium<\/jats:italic>\n species have lost\n \n \n \u03b1<\/mml:mi>\n <\/mml:math>\n <\/jats:inline-formula>\n TAT, and K40 has been replaced by glutamine (Q40), a residue that can mimic acetylated lysine. Here, we investigate the role of microtubule acetylation in apicomplexan parasites by generating and characterizing genetic mutants in\n Plasmodium berghei<\/jats:italic>\n and\n Toxoplasma gondii<\/jats:italic>\n . In\n Plasmodium berghei<\/jats:italic>\n , introduction of a Q40K mutation in\n \n \n \u03b1<\/mml:mi>\n <\/mml:math>\n <\/jats:inline-formula>\n 1 tubulin did not affect parasite development or infectivity, suggesting that the absence of K40 acetylation is not detrimental. In\n Toxoplasma gondii<\/jats:italic>\n , we confirmed that\n \n \n \u03b1<\/mml:mi>\n <\/mml:math>\n <\/jats:inline-formula>\n TAT is responsible for microtubule acetylation but, contrary to previous reports, its deletion had no impact on parasite growth\n in vitro<\/jats:italic>\n . Together, these results indicate that luminal K40 acetylation is not essential for microtubule function in either species, pointing to functional redundancy and highlighting the plasticity of cytoskeletal regulation in apicomplexan parasites.\n <\/jats:p>","DOI":"10.15698\/mic2025.12.863","type":"journal-article","created":{"date-parts":[[2026,1,12]],"date-time":"2026-01-12T21:05:37Z","timestamp":1768251937000},"page":"299-313","source":"Crossref","is-referenced-by-count":3,"title":["Luminal acetylation of microtubules is not essential for Plasmodium berghei and Toxoplasma gondii survival"],"prefix":"10.15698","volume":"12","author":[{"given":"Thrishla","family":"Kumar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katharina","family":"R\u00f6ver","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Johannes 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