APPW2025 参加報告
佐々木 凜芽さん
この度は、幕張メッセで開催されたAPPW2025にて、ポスター発表をさせていただきました。初めての学会発表で緊張しましたが、自分と同じ分野の研究をされている方々と交流し、自らの研究テーマに関する考えを広げることができました。また、今年は解剖学会、生理学会、薬理学会の合同大会であったため、学会会期中に多岐にわたる分野の方々の講演を聞くことができ、最先端の基礎研究について多くの学びを得ることができました。
今回の発表に際してご指導、ご支援いただきました小田教授、久保先生はじめ解剖学講座構造生物学教室の皆様、ライフサイエンスコース事務局の皆様に、深く御礼申し上げます。
以下は発表の抄録です。
Tubulins undergo several posttranslational modifications (PTMs) such as acetylation, polyglutamylation, glycylation, methylation, and phosphorylation, which contribute to the functional diversity of microtubules. Specifically, tubulin PTMs are known to be involved in the function of cilia and flagella (interchangeable terms), but their precise roles remain unclear. In this study, we investigated the significance of tubulin acetylation by examining a novel Chlamydomonas mutant lacking a-tubulin acetyltransferase 1 (aTAT1), an enzyme responsible for acetylating lysine (K) 40 of a-tubulin. The atat1 mutant completely lacked acetylation of a-tubulin in both the axoneme and the cytoplasm, indicating that aTAT1 is the sole enzyme responsible for acetylation of a-tubulin K40 in Chlamydomonas. This expression pattern of tubulin acetyltransferase is consistent with that observed in mammals. By localizing HA-tagged aTAT1, we found that aTAT1 proteins are concentrated at the flagellar tip, likely via a system called the intraflagellar transport. Unexpectedly, the number and length of cytoplasmic microtubules were abnormally increased in the atat1 mutant. Additionally, the atat1 mutant assembled significantly longer flagella in the presence of protein-synthesis inhibitor after deflagellation. These results suggest that the atat1 cytoplasm contains more available tubulin for flagellar assembly compared to the wild-type cytoplasm. Because removal of tubulin acetylation is known to destabilize microtubules, we hypothesize that the cytoplasmic microtubules may serve as a buffer for the excess tubulin resulting from the rapid turnover of non-acetylated form of a-tubulin in the atat1 axoneme.
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Undergraduate Poster Awardを受賞
おめでとうございます！
