Brouhard Gary J, Rice Luke M
Department of Biology, McGill University, Montréal, Quebec, Canada H3A1B1
Department of Biophysics and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390 Department of Biophysics and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390
J Cell Biol. 2014 Nov 10;207(3):323-34. doi: 10.1083/jcb.201407095.
Microtubules are dynamic polymers of αβ-tubulin that form diverse cellular structures, such as the mitotic spindle for cell division, the backbone of neurons, and axonemes. To control the architecture of microtubule networks, microtubule-associated proteins (MAPs) and motor proteins regulate microtubule growth, shrinkage, and the transitions between these states. Recent evidence shows that many MAPs exert their effects by selectively binding to distinct conformations of polymerized or unpolymerized αβ-tubulin. The ability of αβ-tubulin to adopt distinct conformations contributes to the intrinsic polymerization dynamics of microtubules. αβ-Tubulin conformation is a fundamental property that MAPs monitor and control to build proper microtubule networks.
微管是由αβ-微管蛋白组成的动态聚合物,形成多种细胞结构,如用于细胞分裂的有丝分裂纺锤体、神经元的骨架和轴丝。为了控制微管网络的结构,微管相关蛋白(MAPs)和运动蛋白调节微管的生长、收缩以及这些状态之间的转变。最近的证据表明,许多MAPs通过选择性地结合聚合或未聚合的αβ-微管蛋白的不同构象来发挥作用。αβ-微管蛋白采用不同构象的能力有助于微管的内在聚合动力学。αβ-微管蛋白构象是MAPs监测和控制以构建合适微管网络的基本属性。