期刊
JOURNAL OF CELL BIOLOGY
卷 159, 期 1, 页码 55-67出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200204163
关键词
nuclear protein import; importin beta; transportin; nucleoporin; Ran
类别
资金
- NIGMS NIH HHS [GM41955, R01 GM041955] Funding Source: Medline
Previous work has shown that the transport of some small protein cargoes through the nuclear pore complex (NPC) can occur in vitro in the absence of nucleoside triphosphate hydrolysis. We now demonstrate that in the importin alpha/beta and transportin import pathways, efficient in vitro transport of large proteins, in contrast to smaller proteins, requires hydrolyzable GTP and the small GTpase Ran. Morphological and biochemical analysis indicates that the presence of Ran and GTP allows large cargo to efficiently cross central regions of the NPC. We further demonstrate that this function of RanGTP at least partly involves its direct binding to importin P and transportin. We suggest that RanGTP functions in these pathways to promote the transport of large cargo by enhancing the ability of import complexes to traverse diffusionally restricted areas of the NPC.
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