Journal
CELL REPORTS
Volume 31, Issue 8, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2020.107693
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Funding
- Faculty of Arts and Science, University of Toronto
- Canadian Institutes of Health Research [FDN-148399]
- U.S. National Institutes of Health Research [R01 AG061706]
- fellowship (NSERC CGS-D) from the Natural Sciences and Engineering Research Council of Canada
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The mammalian mRNA nuclear export process is thought to terminate at the cytoplasmic face of the nuclear pore complex through ribonucleoprotein remodeling. We conduct a stringent affinity-purification massspectrometry-based screen of the physical interactions of human RNA-binding E3 ubiquitin ligases. The resulting protein-interaction network reveals interactions between the RNA-binding E3 ubiquitin ligase MKRN2 and GLE1, a DEAD-box helicase activator implicated in mRNA export termination. We assess MKRN2 epistasis with GLE1 in a zebrafish model. Morpholino-mediated knockdown or CRISPR/Cas9-based knockout of MKRN2 partially rescue retinal developmental defects seen upon GLE1 depletion, consistent with a functional association between GLE1 and MKRN2. Using ribonomic approaches, we show that MKRN2 binds selectively to the 3' UTR of a diverse subset of mRNAs and that nuclear export of MKRN2-associated mRNAs is enhanced upon knockdown of MKRN2. Taken together, we suggest that MKRN2 interacts with GLE1 to selectively regulate mRNA nuclear export and retinal development.
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