近日，德国萨尔兰大学Laura Schaedel团队揭示了Tau加速微管晶格中的微管蛋白交换。2025年9月4日出版的《自然—物理学》杂志发表了这项成果。

微管是细胞骨架细丝，其特征是尖端的动态不稳定和动态晶格，经历持续的微管蛋白损失和掺入。Tau是一种神经元微管相关蛋白，以其稳定微管尖端和促进微管捆绑的作用而闻名。

研究组证明了tau也调节微管晶格动力学。虽然tau缺乏酶活性，但它显著加速了晶格内的微管蛋白交换，特别是在拓扑缺陷位点。该研究结果表明，tau通过稳定纵向微管蛋白-微管蛋白相互作用而破坏横向相互作用来增强晶格各向异性，从而增强晶格缺陷的迁移性和湮灭性。这些结果挑战了tau蛋白仅仅作为被动稳定剂的传统观点，揭示了其在动态重塑微管晶格结构中的积极作用。

附：英文原文

Title: Tau accelerates tubulin exchange in the microtubule lattice

Author: Biswas, Subham, Grover, Rahul, Reuther, Cordula, Poojari, Chetan S., Shaebani, Reza, Nandakumar, Shweta, Grnewald, Mona, Zablotsky, Amir, Hub, Jochen S., Diez, Stefan, John, Karin, Schaedel, Laura

Issue&Volume: 2025-09-04

Abstract: Microtubules are cytoskeletal filaments characterized by dynamic instability at their tips and a dynamic lattice that undergoes continuous tubulin loss and incorporation. Tau, a neuronal microtubule-associated protein, is well known for its role in stabilizing microtubule tips and promoting microtubule bundling. Here we demonstrate that tau also modulates microtubule lattice dynamics. Although tau lacks enzymatic activity, it significantly accelerates tubulin exchange within the lattice, particularly at topological defect sites. Our findings indicate that tau enhances lattice anisotropy by stabilizing longitudinal tubulin–tubulin interactions while destabilizing lateral ones, thereby enhancing the mobility and annihilation of lattice defects. These results challenge the traditional view of tau as merely a passive stabilizer, revealing its active role in dynamically remodelling the microtubule lattice structure.

DOI: 10.1038/s41567-025-03003-7

Source: https://www.nature.com/articles/s41567-025-03003-7