Intraflagellar transport in the unicellular green alga, Chlamydomonas reinhardtii.
Intraflagellar transport in the unicellular green alga, Chlamydomonas reinhardtii.
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单细胞绿藻莱茵衣藻的鞭毛内运输。
DOI：
10.1078/143446103322166491
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发表时间：
2003
期刊：
影响因子：
2.5
通讯作者：
Cole,DouglasG
中科院分区：
文献类型：
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作者：
Cole,DouglasG
双鞭毛虫、绿藻、莱茵衣藻已被证明是研究鞭毛内运输（FT）最高产的模式生物，将是本文的重点。| FT是大蛋白颗粒沿真核纤毛和鞭毛轴突微管的双向运动。仅在十年前，当使用视频增强差分干涉对比（D1C）显微镜观察衣藻时，首次记录了IFT颗粒的运动（Kozminski et al. 1993）。在DIC显微镜下，可以看到双折射脉冲沿着鞭毛向两个方向移动。仅仅十年后，该领域迅速发展，我们发现lFT是一个古老而保守的过程，负责运动和非运动纤毛和鞭毛的组装和维护（见Pazour和Rosenbaum 2002； Rosenbaum和Witman 2002； Sloboda 2002）。在kinein - il的驱动下，顺行IFT是指蛋白质颗粒从鞭毛基部向远端移动，而细胞质动力蛋白1b负责颗粒逆行移动回细胞体（图1）。在衣藻中，lFT颗粒是200-300 nm的线性蛋白质复合物阵列，包含至少16种独特的多肽，可以分离为两个相对较小的复合物，A和B （Cole et al. 1998; Piperno and Mead 1997）。序列分析表明，该颗粒蛋白具有丰富的蛋白-蛋白结合基序，可用于轴突前体等多种物质的转运。下面简要介绍了衣藻的lFT马达和颗粒蛋白，并对其可能的生物学功能进行了讨论。
The biflagellate, green alga, Chlamydomonas reinhardtii has proven to be the most productive model organism for the study of intraflagellar transport (FT) and will serve as the focus Of this review.| FT js the bidirectional movement of large protein particles along axonemal microtubules of eukaryotic cilia and flagella. The movement of IFT particles was first documented only a decade ago when Chlamydomonas was observed using video-enhanced differential interference contrast (D1C) microscopy (Kozminski et al. 1993). With DIC microscopy, birefringent pulses could be seen moving along the flagellum in both directions. Just ten years later, the field has rapidly evolved and we find that lFT is an ancient and conserved process responsible for the assembly and maintenance of both motile and nonmotile cilia and flagella (reviewed in Pazour and Rosenbaum 2002; Rosenbaum and Witman 2002; Sloboda 2002).Driven by kinesin-Il, anterograde IFT is the move-ment of protein particles from the base of the flagellum out to the distal tip while cytoplasmic dynein 1b is responsible for the retrograde movement of particles back to the cell body (Fig. 1). In Chlamydomonas, the lFT particles are 200–300 nm linear arrays of protein complexes containing at least 16 unique polypeptides that can be isolated as two relatively small complexes, A and B (Cole et al. 1998; Piperno and Mead 1997). Sequence analysis reveals that the particle proteins are rich in protein-protein binding motifs, which could be used in the transport of various cargoes such as axonemal precursors. What follows is a brief description of the lFT motors and particle proteins of Chlamydomonas and a discussion regarding possible biological functions of IFT.