This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hutten, S.
Right arrow Articles by Kehlenbach, R. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hutten, S.
Right arrow Articles by Kehlenbach, R. H.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, September 2006, p. 6772-6785, Vol. 26, No. 18
0270-7306/06/$08.00+0     doi:10.1128/MCB.00342-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Nup214 Is Required for CRM1-Dependent Nuclear Protein Export In Vivo

Saskia Hutten1,2 and Ralph H. Kehlenbach1,2*

Abteilung Virologie, Universität Heidelberg, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany,1 Zentrum für Biochemíe und Molekulare Zellbiologie, Universität Göttingen, Humboldtallee 23, 37073 Göttingen, Germany2

Received 24 February 2006/ Returned for modification 24 March 2006/ Accepted 30 June 2006

Nucleoporins mediate transport of macromolecules across the nuclear pore complex, yet the function of many individual nucleoporins is largely unresolved. To address this question, we depleted cells of the cytoplasmic nucleoporins Nup214/CAN and Nup358/RanBP2 by RNA interference. Depletion of Nup214 resulted in codepletion of its binding partner, Nup88. Nuclear pore complexes assembled in the absence of Nup214/Nup88 or Nup358 were fully functional in nuclear protein import, whereas nuclear mRNA export was slightly impaired. Depletion of Nup358 had only a minor effect on nuclear protein export. In contrast, depletion of Nup214/Nup88 led to strongly reduced CRM1-mediated export of the shuttling transcription factor NFAT as well as a human immunodeficiency virus-Rev derivative. A specific role of Nup214 in protein export is furthered by the biochemical properties of a high-affinity complex containing Nup214, CRM1, RanGTP, and an export cargo. Our results show that the Nup214/Nup88 complex is required for efficient CRM1-mediated transport, supporting a model involving a high-affinity binding site for CRM1 at Nup214 in the terminal steps of export.

* Corresponding author. Present address: Universität Göttingen, Zentrum für Biochemie und Molekulare Zellbiologie, Humboldtallee 23, 37073 Göttingen, Germany. Phone: 49-551-395950. Fax: 49-551-395960. E-mail: rkehlen{at}gwdg.de.

Molecular and Cellular Biology, September 2006, p. 6772-6785, Vol. 26, No. 18
0270-7306/06/$08.00+0     doi:10.1128/MCB.00342-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Zolotukhin, A. S., Uranishi, H., Lindtner, S., Bear, J., Pavlakis, G. N., Felber, B. K. (2009). Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA. Nucleic Acids Res 0: gkp782v1-gkp782 [Abstract] [Full Text]  
  • Murawala, P., Tripathi, M. M., Vyas, P., Salunke, A., Joseph, J. (2009). Nup358 interacts with APC and plays a role in cell polarization. J. Cell Sci. 122: 3113-3122 [Abstract] [Full Text]  
  • Pasdeloup, D., Blondel, D., Isidro, A. L., Rixon, F. J. (2009). Herpesvirus Capsid Association with the Nuclear Pore Complex and Viral DNA Release Involve the Nucleoporin CAN/Nup214 and the Capsid Protein pUL25. J. Virol. 83: 6610-6623 [Abstract] [Full Text]  
  • Hutten, S., Walde, S., Spillner, C., Hauber, J., Kehlenbach, R. H. (2009). The nuclear pore component Nup358 promotes transportin-dependent nuclear import. J. Cell Sci. 122: 1100-1110 [Abstract] [Full Text]  
  • Copeland, A. M., Newcomb, W. W., Brown, J. C. (2009). Herpes Simplex Virus Replication: Roles of Viral Proteins and Nucleoporins in Capsid-Nucleus Attachment. J. Virol. 83: 1660-1668 [Abstract] [Full Text]  
  • Andres-Hernando, A., Lanaspa, M. A., Rivard, C. J., Berl, T. (2008). Nucleoporin 88 (Nup88) Is Regulated by Hypertonic Stress in Kidney Cells to Retain the Transcription Factor Tonicity Enhancer-binding Protein (TonEBP) in the Nucleus. J. Biol. Chem. 283: 25082-25090 [Abstract] [Full Text]  
  • Hutten, S., Flotho, A., Melchior, F., Kehlenbach, R. H. (2008). The Nup358-RanGAP Complex Is Required for Efficient Importin {alpha}/{beta}-dependent Nuclear Import. Mol. Biol. Cell 19: 2300-2310 [Abstract] [Full Text]  
  • Dultz, E., Zanin, E., Wurzenberger, C., Braun, M., Rabut, G., Sironi, L., Ellenberg, J. (2008). Systematic kinetic analysis of mitotic dis- and reassembly of the nuclear pore in living cells. JCB 180: 857-865 [Abstract] [Full Text]  
  • Resendes, K. K., Rasala, B. A., Forbes, D. J. (2008). Centrin 2 Localizes to the Vertebrate Nuclear Pore and Plays a Role in mRNA and Protein Export. Mol. Cell. Biol. 28: 1755-1769 [Abstract] [Full Text]  
  • Sabri, N., Roth, P., Xylourgidis, N., Sadeghifar, F., Adler, J., Samakovlis, C. (2007). Distinct functions of the Drosophila Nup153 and Nup214 FG domains in nuclear protein transport. JCB 178: 557-565 [Abstract] [Full Text]  
  • Qu, J., Liu, G.-H., Huang, B., Chen, C. (2007). Nitric oxide controls nuclear export of APE1/Ref-1 through S-nitrosation of Cysteines 93 and 310. Nucleic Acids Res 35: 2522-2532 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»