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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-3C04-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-BCFF-9
Genre: Journal Article

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Deane, R., Author
Schäfer, W., Author
Zimmermann, H. P., Author
Mueller, L., Author
Görlich, D.1, Author              
Prehn, S., Author
Ponstingl, H., Author
Bischoff, F. R., Author
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1Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society, ou_578574              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 1997-09
 Publication Status: Published in print
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Title: Molecular and Cellular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 17 (9) Sequence Number: - Start / End Page: 5087 - 5096 Identifier: -