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Abstract：
The ciliary tip has been implicated in ciliary assembly and disassembly, and signaling, yet information on its protein composition is limited. Using comparative, quantitative proteomics based on the fact that tip proteins will be approximately twice as concentrated in half-length compared with full-length flagella, we have identified FAP256 as a tip protein in Chlamydomonas. FAP256 localizes to the tips of both central pair and outer doublet microtubules (MTs) and it remains at the tip during flagellar assembly and disassembly. Similarly, its vertebrate counterpart, CEP104, localizes on the distal ends of both centrioles of nondividing cells until the mother centriole forms a cilium and then localizes at the tip of the elongating cilium. A null mutant of FAP256 in Chlamydomonas and RNAi in vertebrate cells showed that FAP256/CEP104 is required for ciliogenesis in a high percentage of cells. In those cells that could form cilia, there were structural deformities at the ciliary tips.
摘要：
睫状尖端与睫状组装和拆卸有关，和信号，然而，关于其蛋白质成分的信息是有限的。使用比较，定量蛋白质组学基于这样一个事实，即尖端蛋白的半长浓度大约是全长鞭毛的两倍，我们已经确定FAP256是衣藻的尖端蛋白。FAP256位于中央对和外部双合微管（MT）的尖端，并且在鞭毛组装和拆卸过程中仍保留在尖端。同样，它的脊椎动物对应物，CEP104位于非分裂细胞的两个中心粒的远端，直到母中心粒形成纤毛，然后位于伸长的纤毛的尖端。衣藻中FAP256的无效突变体和脊椎动物细胞中的RNAi表明FAP256/CEP104是高百分比细胞中的纤毛发生所必需的。在那些可能形成纤毛的细胞中，睫状尖端有结构畸形。
