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  Structural and functional characterization of CRM1-Nup214 interactions reveals multiple FG-binding sites involved in nuclear export.

Port, S. A., Monecke, T., Dickmanns, A., Spillner, C., Hofele, R., Urlaub, H., et al. (2015). Structural and functional characterization of CRM1-Nup214 interactions reveals multiple FG-binding sites involved in nuclear export. Cell Reports, 13(4), 690-702. doi:10.1016/j.celrep.2015.09.042.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-07AE-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-2860-3
Genre: Journal Article

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 Creators:
Port, S. A., Author
Monecke, T., Author
Dickmanns, A., Author
Spillner, C., Author
Hofele, R.1, Author              
Urlaub, H.1, Author              
Ficner, R., Author
Kehlenbach, H., Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: CRM1 is the major nuclear export receptor. During translocation through the nuclear pore, transport complexes transiently interact with phenylalanine-glycine (FG) repeats of multiple nucleoporins. On the cytoplasmic side of the nuclear pore, CRM1 tightly interacts with the nucleoporin Nup214. Here, we present the crystal structure of a 117-amino-acid FG-repeat-containing fragment of Nup214, in complex with CRM1, Snurportin 1, and RanGTP at 2.85 angstrom resolution. The structure reveals eight binding sites for Nup214 FG motifs on CRM1, with intervening stretches that are loosely attached to the transport receptor. Nup214 binds to N- and C-terminal regions of CRM1, thereby clamping CRM1 in a closed conformation and stabilizing the export complex. The role of conserved hydrophobic pockets for the recognition of FG motifs was analyzed in biochemical and cell-based assays. Comparative studies with RanBP3 and Nup62 shed light on specificities of CRM1-nucleoporin binding, which serves as a paradigm for transport receptor-nucleoporin interactions.

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Language(s): eng - English
 Dates: 2015-10-152015-10-27
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.celrep.2015.09.042
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Title: Cell Reports
Source Genre: Journal
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Pages: - Volume / Issue: 13 (4) Sequence Number: - Start / End Page: 690 - 702 Identifier: -