期刊
JOURNAL OF CELL BIOLOGY
卷 167, 期 4, 页码 583-590出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200407156
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资金
- NIGMS NIH HHS [GM 58065, R01 GM058065] Funding Source: Medline
Nucleocytoplasmic transport occurs through gigantic proteinaceous channels called nuclear pore col plexes (NPCs). Translocation through the NPC is exquisitely selective and is mediated by interactions between soluble transport carriers and insoluble NPC proteins that contain phenylalanine-glycine (FG) repeats. Although most FG nucleoporins (Nups) are organized symmetrically about the planar axis of the nuclear envelope, very few localize exclusively to one side of the NPC. We constructed Saccharomyces cerevisiae mutants with asymmetric FG repeats either deleted or swapped to generate NPCs with inverted FG asymmetry. The mutant Nups localize properly within the NPC and exhibit exchanged binding specificity for the export factor Xpo1. Surprisingly, we were unable to detect any defects in the Kap95, Kap121, Xpo1, or mRNA transport pathways in cells expressing the mutant FG Nups. These findings suggest that the biased distribution of FG repeats is not required for major nucleocytoplasmic trafficking events across the NPC.
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