Function of tubulin polyglutamylation in cilia/flagella motility mechanism

为了探讨微管蛋白多谷氨酰化在纤毛/鞭毛运动中的作用，我们研究了一株缺乏微管蛋白多聚谷氨酰化酶(TTLL9)的衣藻突变体tpg1的运动特性。在tpg1和各种动力蛋白缺失突变体之间的双突变体的运动性分析表明，在10多种轴线动力蛋白中，长链微管蛋白多谷氨酸化只影响一种特定的动力蛋白--内臂动力蛋白的功能。此外，使用另一个突变体tpg2的研究表明，一种名为FAP234的蛋白质在TTLL9的运输和稳定中发挥作用。

To approach the function of tubulin polyglutamylation in cilia/flagella motility, we examined the motile properties of a Chlamydomonas tpg1, a mutant that lacks a tubulin polygultamylating enzyme (TTLL9). Motility analyses in double mutants between tpg1 and various kinds of dynein-deficient mutants revealed that long-chain tubulin polyglutamylation affects the function of only one particular species of dynein, inner arm dynein e, among more than 10 species of axonemal dyneins. Furthermore, studies using another mutant, tpg2, showed that a protein designated FAP234 functions in the transport and stabilization of TTLL9.