Functional and molecular diversity of dynein heavy chains
Functional and molecular diversity of dynein heavy chains
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动力蛋白重链的功能和分子多样性
DOI：
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发表时间：
1996
期刊：
影响因子：
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通讯作者：
D. J. Asai
中科院分区：
文献类型：
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作者：
D. J. Asai
动力蛋白沿着微管的定向移位是多种细胞运动的基础。在真核生物的鞭毛和纤毛中，动力蛋白产生外双微管的主动滑动，这是轴丝弯曲的基础。几种动力蛋白重链同种型精确地位于轴丝中，以引发和传播弯曲，并且据信这些不同的同种型产生不同的剪切力。动力蛋白同种型的序列分析表明，在生产力的专业化可能是动力蛋白催化结构域的蛋白质序列的结果。细胞质动力蛋白的多种亚型的最新证据导致细胞质动力蛋白亚型被单独定制以产生特定的力或携带单独的货物的假设。
Abstract The directed translocation of dynein along microtubules is the basis for a wide variety of essential cellular movements. In eukaryotic flagella and cilia, dynein produces the active sliding of outer doublet microtubules that underlies axonemal bending. Several dynein heavy chain isoforms are precisely located in the axoneme in order to initiate and propagate bends, and it is believed that these different isoforms produce distinct shear forces. Analysis of the sequences of dynein isoforms suggests that the specialization in force production may be a consequence of the protein sequence of the dynein catalytic domain. Recent evidence for multiple isoforms of cytoplasmic dynein leads to the hypothesis that cytoplasmic dynein isoforms are individually tailored to produce specific forces or to carry separate cargoes.