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Updated: Oct 8, 2025

TRAP-rc, Translating Ribosome Affinity Purification from Rare Cell Populations of Drosophila Embryos
Published on: September 10, 2015
Association of RanGAP to nuclear pore complex component, RanBP2/Nup358, is required for pupal development in
Shane Chen1, Maria Lyanguzova1, Ross Kaufhold1
1Division of Molecular and Cellular Biology, National Institutes for Child Health and Human Development, 49 Convent Drive, Building 49, Room 5A30, Bethesda, MD 20892, USA.
Abstract:
Ran's GTPase-activating protein (RanGAP) is tethered to the nuclear envelope (NE) in multicellular organisms. We investigated the consequences of RanGAP localization in human tissue culture cells and Drosophila. In tissue culture cells, disruption of RanGAP1 NE localization surprisingly has neither obvious impacts on viability nor nucleocytoplasmic transport of a model substrate. In Drosophila, we identified a region within nucleoporin dmRanBP2 required for direct tethering of dmRanGAP to the NE. A dmRanBP2 mutant lacking this region shows no apparent growth defects during larval stages but arrests at the early pupal stage. A direct fusion of dmRanGAP to the dmRanBP2 mutant rescues this arrest, indicating that dmRanGAP recruitment to dmRanBP2 per se is necessary for the pupal ecdysis sequence. Our results indicate that while the NE localization of RanGAP is widely conserved in multicellular organisms, the targeting mechanisms are not. Further, we find a requirement for this localization during pupal development.
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