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Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor importin-beta but interacts differently with RanBP1.

MPG-Autoren
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Görlich,  D.
Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society;

Externe Ressourcen

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC232359/pdf/175087.pdf
(Verlagsversion)

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1922653.pdf
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Zitation

Deane, R., Schäfer, W., Zimmermann, H. P., Mueller, L., Görlich, D., Prehn, S., et al. (1997). Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor importin-beta but interacts differently with RanBP1. Molecular and Cellular Biology, 17(9), 5087-5096.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0015-3C04-6
Zusammenfassung
We report the identification and characterization of a novel 124-kDa Ran binding protein, RanBP5. This protein is related to importin-beta, the key mediator of nuclear localization signal (NLS)-dependent nuclear transport. RanBP5 was identified by two independent methods: it was isolated from HeLa cells by using its interaction with RanGTP in an overlay assay to monitor enrichment, and it was also found by the yeast two-hybrid selection method with RanBP1 as bait. RanBP5 binds to RanBP1 as part of a trimeric RanBP1-Ran-RanBP5 complex. Like importin-beta, RanBP5 strongly binds the GTP-bound form of Ran, stabilizing it against both intrinsic and RanGAP1-induced GTP hydrolysis and also against nucleotide exchange. The GAP resistance of the RanBP5-RanGTP complex can be relieved by RanBP1, which might reflect an in vivo role for RanBP1. RanBP5 is a predominantly cytoplasmic protein that can bind to nuclear pore complexes. We propose that RanBP5 is a mediator of a nucleocytoplasmic transport pathway that is distinct from the importin-alpha-dependent import of proteins with a classical NLS.