Journal
JOURNAL OF CELL BIOLOGY
Volume 178, Issue 7, Pages 1121-1132Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200704174
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Funding
- NCI NIH HHS [5T32-CA009385, T32 CA009385] Funding Source: Medline
- NIGMS NIH HHS [R01 GM051219, R01-GM51219] Funding Source: Medline
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Trafficking of nucleic acids and large proteins through nuclear pore complexes (NPCs) requires interactions with NPC proteins that harbor FG (phenylalanineglycine) repeat domains. Specialized transport receptors that recognize cargo and bind FG domains facilitate these interactions. Whether different transport receptors utilize preferential FG domains in intact NPCs is not fully resolved. In this study, we use a large-scale deletion strategy in Saccharomyces cerevisiae to generate a new set of more minimal pore (mmp) mutants that lack specific FG domains. A comparison of messenger RNA (mRNA) export versus protein import reveals unique subsets of mmp mutants with functional defects in specific transport receptors. Thus, multiple functionally independent NPC translocation routes exist for different transport receptors. Our global analysis of the FG domain requirements in mRNA export also finds a requirement for two NPC substructures-one on the nuclear NPC face and one in the NPC central core. These results pinpoint distinct steps in the mRNA export mechanism that regulate NPC translocation efficiency.
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