Journal
JOURNAL OF CELL BIOLOGY
Volume 211, Issue 6, Pages 1121-1130Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201503135
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Funding
- National Institutes of Health [GM57071, GM058065]
- Canadian Institutes of Health Research [MOP130231]
- Canada Research Chairs program
- Alberta Innovates Technology Futures Graduate Scholarship
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Many messenger RNA export proteins have been identified; yet the spatial and temporal activities of these proteins and how they determine directionality of messenger ribonucleoprotein (mRNP) complex export from the nucleus remain largely undefined. Here, the bacteriophage PP7 RNA-labeling system was used in Saccharomyces cerevisiae to follow single-particle mRNP export events with high spatial precision and temporal resolution. These data reveal that mRNP export, consisting of nuclear docking, transport, and cytoplasmic release from a nuclear pore complex (NPC), is fast (similar to 200 ms) and that upon arrival in the cytoplasm, mRNPs are frequently confined near the nuclear envelope. Mex67p functions as the principal mRNP export receptor in budding yeast. In a mex67-5 mutant, delayed cytoplasmic release from NPCs and retrograde transport of mRNPs was observed. This proves an essential role for Mex67p in cytoplasmic mRNP release and directionality of transport.
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