Role of a class DHC1b dynein in retrograde transport of IFT motors and IFT raft particles along cilia, but not dendrites, in chemosensory neurons of living Caenorhabditis elegans

被引:233
作者
Signor, D
Wedaman, KP
Orozco, JT
Dwyer, ND
Bargmann, CI
Rose, LS
Scholey, JM
机构
[1] Univ Calif Davis, Sect Mol & Cellular Biol, Davis, CA 95616 USA
[2] Univ Calif San Francisco, Howard Hughes Med Inst, Dept Anat, San Francisco, CA 94143 USA
关键词
dynein; kinesin; intraflagellar transport; Caenorhabditis elegans; neuron transport;
D O I
10.1083/jcb.147.3.519
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The heterotrimeric motor protein, kinesin-II, and its presumptive cargo. can be observed moving anterogradely at 0.7 mu m/s by intraflagellar transport (IF-T) within sensory cilia of chemosensory neurons of living Caenorhabditis elegans! using a fluorescence microscope-based transport assay (Orozco, J.T., K.P. Wedaman, D. Signor, H. Brown, L. Rose, and J.M. Scholey. 1999. Nature. 398:674). Here, we report that kinesin-II, and two of its presumptive cargo molecules, OSM-1 and OSM-6, all move at similar to 1.1 mu m/s in the retrograde direction along cilia and dendrites, which is consistent with the hypothesis that these proteins are retrieved from the distal endings of the cilia by a retrograde transport pathway that moves them along cilia and then dendrites, back to the neuronal cell body. To test the hypothesis that the minus end-directed microtubule motor protein, cytoplasmic dynein, drives this retrograde transport pathway, we visualized movement of kinesin-II and its cargo along dendrites and cilia in a che-3 cytoplasmic dynein mutant background, and observed an inhibition of retrograde transport in cilia but not in dendrites. In contrast, anterograde IFT proceeds normally in che-3 mutants. Thus, we propose that the class DHC1b cytoplasmic dynein, CHE-3, is specifically responsible for the retrograde transport of the anterograde motor, kinesin-II, and its cargo within sensory cilia, but not within dendrites.
引用
收藏
页码:519 / 530
页数:12
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