The RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependent nuclear export complexes

Tobias Ritterhoff, Hrishikesh Das, Götz Hofhaus, Rasmus R. Schröder, Annette Flotho and Frauke Melchior ()
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Tobias Ritterhoff: Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance
Hrishikesh Das: Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance
Götz Hofhaus: Cryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg
Rasmus R. Schröder: Cryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg
Annette Flotho: Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance
Frauke Melchior: Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: Abstract Continuous cycles of nucleocytoplasmic transport require disassembly of transport receptor/Ran-GTP complexes in the cytoplasm. A basic disassembly mechanism in all eukaryotes depends on soluble RanGAP and RanBP1. In vertebrates, a significant fraction of RanGAP1 stably interacts with the nucleoporin RanBP2 at a binding site that is flanked by FG-repeats and Ran-binding domains, and overlaps with RanBP2’s SUMO E3 ligase region. Here, we show that the RanBP2/RanGAP1*SUMO1/Ubc9 complex functions as an autonomous disassembly machine with a preference for the export receptor Crm1. We describe three in vitro reconstituted disassembly intermediates, which show binding of a Crm1 export complex via two FG-repeat patches, cargo-release by RanBP2’s Ran-binding domains and retention of free Crm1 at RanBP2 after Ran-GTP hydrolysis. Intriguingly, all intermediates are compatible with SUMO E3 ligase activity, suggesting that the RanBP2/RanGAP1*SUMO1/Ubc9 complex may link Crm1- and SUMO-dependent functions.

Date: 2016
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DOI: 10.1038/ncomms11482

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