Inaba Hiroshi, Kageyama Daichi, Watari Soei, Tateishi Mahoko, Kakugo Akira, Matsuura Kazunori
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University Tottori 680-8552 Japan
Center for Research on Green Sustainable Chemistry, Tottori University Tottori 680-8552 Japan.
RSC Chem Biol. 2025 Mar 19;6(5):737-745. doi: 10.1039/d4cb00290c. eCollection 2025 May 8.
Microtubules are major cytoskeletons involved in various cellular functions, such as regulating cell shape and division and cargo transport motor proteins. In addition to widely studied singlet microtubules, complex microtubule superstructures, including doublets and bundles, provide unique mechanical and functional properties . However, a method to construct such superstructures remains unresolved. This study presents a peptide-based approach for constructing microtubule superstructures by displaying Tau-derived peptides (TP) on the outer surface of microtubules using KA7 peptides as binding units. The KA7-connected TP (KA7-TP) bound to the -terminal tail on the outer surface of microtubules and induced doublets and bundles by recruiting tubulin. Notably, the outer layers of the doublet microtubules generated by KA7-TP dissociated, highlighting the utility of this approach for studying the formation/dissociation mechanisms of microtubule superstructures. The simple peptide-based approach facilitates our understanding of microtubule superstructures and offers new opportunities for applying microtubule superstructures to nanotechnology.
微管是参与多种细胞功能的主要细胞骨架，如调节细胞形状、分裂以及货物运输的驱动蛋白。除了被广泛研究的单微管外，复杂的微管超结构，包括双微管和微管束，具有独特的机械和功能特性。然而，构建这种超结构的方法仍未得到解决。本研究提出了一种基于肽的方法来构建微管超结构，即使用KA7肽作为结合单元，将Tau衍生肽（TP）展示在微管外表面。与KA7相连的TP（KA7-TP）与微管外表面的α-末端尾部结合，并通过招募微管蛋白诱导形成双微管和微管束。值得注意的是，由KA7-TP产生的双微管的外层会解离，这突出了该方法在研究微管超结构形成/解离机制方面的实用性。这种基于肽的简单方法有助于我们理解微管超结构，并为将微管超结构应用于纳米技术提供了新的机会。
