Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex.

Terry LJ, Wente SR
J Cell Biol. 2007 178 (7): 1121-32

PMID: 17875746 · PMCID: PMC2064648 · DOI:10.1083/jcb.200704174

Trafficking of nucleic acids and large proteins through nuclear pore complexes (NPCs) requires interactions with NPC proteins that harbor FG (phenylalanine-glycine) 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.

MeSH Terms (19)

Active Transport, Cell Nucleus beta Karyopherins Cell Nucleus Mutation Nuclear Pore Nuclear Pore Complex Proteins Nuclear Proteins Nucleocytoplasmic Transport Proteins Poly A Protein Binding Protein Structure, Tertiary Protein Transport RNA, Messenger RNA-Binding Proteins RNA Transport Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Structure-Activity Relationship Temperature

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