Protein transport to the dendritic plasma membrane of cultured neurons is regulated by rab8p.

Protein transport to the dendritic plasma membrane of cultured neurons is regulated by rab8p.
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DOI:
10.1083/jcb.123.1.47
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发表时间:
1993-10
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Dotti C
Dotti C
中科院分区:
其他
文献类型:
--
作者:
Huber LA;de Hoop MJ;Dupree P;Zerial M;Simons K;Dotti C

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在合著的论文中(Huber, l.a., s.w. Pimplikar, r.g. Parton, H. Virta, M. Zerial和K. Simons)。J. Cell Biol. 123:35-45),我们报道了小GTPase rab8p参与了从TGN到上皮基底外侧质膜的运输。本研究探讨了rab8p在极化海马神经元中的定位和功能。通过免疫荧光显微镜我们发现rab8p优先定位于体树突结构域,而被排除在轴突之外。双标记免疫荧光显示部分rab8p与塞姆利基森林病毒糖蛋白E2 (SFV-E2)在树突上共定位。采用反义寡核苷酸方法研究rab8p在新合成的病毒糖蛋白树突转运中的作用。将rab8编码序列起始区对应的反义寡核苷酸加入培养的神经元中4天。这种处理导致rab8p的细胞水平显著降低,SFV- E2从细胞体到树突的转运显著减少。然而,对流感HA的轴突转运没有影响。从这些结果我们推断rab8p参与了蛋白质向神经元树突表面的转运。
In the companion paper (Huber, L. A., S. W. Pimplikar, R. G. Parton, H. Virta, M. Zerial, and K. Simons. J. Cell Biol. 123:35-45) we reported that the small GTPase rab8p is involved in transport from the TGN to the basolateral plasma membrane in epithelia. In the present work we investigated the localization and function of rab8p in polarized hippocampal neurons. By immunofluorescence microscopy we found that rab8p localized preferentially in the somatodendritic domain, and was excluded from the axon. Double-labeling immunofluorescence showed that some of the rab8p co-localized in the dendrites with the Semliki Forest Virus glycoprotein E2 (SFV-E2). An antisense oligonucleotide approach was used to investigate the role of rab8p in dendritic transport of newly synthesized viral glycoproteins. Antisense oligonucleotides corresponding to the initiation region of the rab8 coding sequence were added to the cultured neurons for four days. This treatment resulted in a significant decrease in cellular levels of rab8p and transport of SFV- E2 from the cell body to the dendrites was significantly reduced. However, no effect was observed on axonal transport of influenza HA. From these results we conclude that rab8p is involved in transport of proteins to the dendritic surface in neurons.