Cole Douglas G
Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, Idaho, 83844-3052, USA.
Traffic. 2003 Jul;4(7):435-42. doi: 10.1034/j.1600-0854.2003.t01-1-00103.x.
First discovered in the green alga, Chlamydomonas, intraflagellar transport (IFT) is the bidirectional movement of protein particles along the length of eukaryotic cilia and flagella. Composed of approximately 16 different proteins, IFT particles are moved out to the distal tip of the organelle by kinesin-II and are brought back to the cell body by cytoplasmic dynein 1b. Mutant analysis of the IFT motor and particle proteins using diverse organisms has revealed a conserved and essential role for IFT in the assembly and maintenance of cilia and flagella. IFT is thought to mediate this assembly through the delivery of axonemal precursors out to the distal tip of the growing organelle. Consistent with this model, the IFT particle proteins are rich in protein-protein binding motifs, suggesting that the particles may act as scaffolds for the binding of multiple cargoes. With most of the IFT proteins now identified at the level of the gene, this review will briefly examine both the structure and function of the IFT machinery of Chlamydomonas reinhardtii.
鞭毛内运输（IFT）最初是在绿藻衣藻中发现的，它是蛋白质颗粒沿真核生物纤毛和鞭毛长度的双向移动。IFT颗粒由大约16种不同的蛋白质组成，通过驱动蛋白-II被运送到细胞器的远端，再由细胞质动力蛋白1b带回细胞体。利用多种生物对IFT运动蛋白和颗粒蛋白进行的突变分析表明，IFT在纤毛和鞭毛的组装与维持中具有保守且至关重要的作用。IFT被认为通过将轴丝前体运输到生长中细胞器的远端来介导这种组装。与该模型一致，IFT颗粒蛋白富含蛋白质-蛋白质结合基序，这表明这些颗粒可能作为多种货物结合的支架。由于现在大多数IFT蛋白已在基因水平上得到鉴定，本综述将简要探讨莱茵衣藻IFT机制的结构和功能。
