Post-chaperonin tubulin folding pathway

Alpha and beta tubulin folding intermediates are formed through ATP-dependent interaction with TriC/CCT. In order to form a functional heterodimer, these folding intermediates undergo a series of interactions with five proteins: (cofactors A-E) following release from TriC/CCT (reviewed in Cowan and Lewis et al., 2001). These interactions are described in the reactions below. Ultimately, alpha tubulin, when associated with cofactor E, interacts with cofactor D-bound beta-tubulin. The entry of cofactor C into this complex results in the discharge of native heterodimer triggered by GTP hydrolysis in beta tubulin (Tian et al., 1997).

α和β微管蛋白的折叠中间体通过依赖于ATP与TriC/CCT的相互作用而形成。为了形成功能性的异二聚体，这些折叠中间体在从TriC/CCT释放后，需与五种蛋白（辅因子A-E）进行一系列相互作用（如Cowan和Lewis等人于2001年所综述）。以下反应详细描述了这些相互作用。最终，当α微管蛋白与辅因子E结合时，将与结合辅因子D的β微管蛋白相互作用。辅因子C进入此复合体，导致由β微管蛋白中GTP水解触发的天然异二聚体的释放（参见Tian等人，1997年）。