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Molecular and Cellular Biology, December 2006, p. 8697-8709, Vol. 26, No. 23
0270-7306/06/$08.00+0     doi:10.1128/MCB.00708-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Nuclear Localization Signal and Protein Context both Mediate Importin {alpha} Specificity of Nuclear Import Substrates{triangledown}

Beate Friedrich,1 Christina Quensel,1 Thomas Sommer,1 Enno Hartmann,2 and Matthias Köhler1,3,4*

The Max Delbrueck Center for Molecular Medicine, Robert Roessle Str. 10, 13125 Berlin, Germany,1 Institute of Biology, Center of Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany,2 Nephrology Section, Franz Volhard Clinic, HELIOS Klinikum Berlin, Wiltbergstr. 50, 13125 Berlin, Germany,3 Center for Nephrology and Hypertension, Ostsee Clinic and Reha Clinic Damp, Seute-Deern-Ring 30, 24351 Damp, Germany4

Received 25 April 2006/ Returned for modification 18 May 2006/ Accepted 18 September 2006

The "classical" nuclear protein import pathway depends on importin {alpha} and importin ß. Importin {alpha} binds nuclear localization signal (NLS)-bearing proteins and functions as an adapter to access the importin ß-dependent import pathway. In humans, only one importin ß is known to interact with importin {alpha}, while six {alpha} importins have been described. Various experimental approaches provided evidence that several substrates are transported specifically by particular {alpha} importins. Whether the NLS is sufficient to mediate importin {alpha} specificity is unclear. To address this question, we exchanged the NLSs of two well-characterized import substrates, the seven-bladed propeller protein RCC1, preferentially transported into the nucleus by importin {alpha}3, and the less specifically imported substrate nucleoplasmin. In vitro binding studies and nuclear import assays revealed that both NLS and protein context contribute to the specificity of importin {alpha} binding and transport.

* Corresponding author. Mailing address: Center for Nephrology and Hypertension, Ostsee Clinic and Reha Clinic Damp, Seute-Deern-Ring 30, 24351 Damp, Germany. Phone: 49-4352-808858. Fax: 49-4352-8078858. E-mail: matthias.koehler{at}damp.de.

{triangledown} Published ahead of print on 25 September 2006.

Molecular and Cellular Biology, December 2006, p. 8697-8709, Vol. 26, No. 23
0270-7306/06/$08.00+0     doi:10.1128/MCB.00708-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Pradeepa, M. M., Manjunatha, S., Sathish, V., Agrawal, S., Rao, M. R. S. (2008). Involvement of Importin-4 in the Transport of Transition Protein 2 into the Spermatid Nucleus. Mol. Cell. Biol. 28: 4331-4341 [Abstract] [Full Text]  
  • Terry, L. J., Shows, E. B., Wente, S. R. (2007). Crossing the Nuclear Envelope: Hierarchical Regulation of Nucleocytoplasmic Transport. Science 318: 1412-1416 [Abstract] [Full Text]  
  • Hood, F. E., Clarke, P. R. (2007). RCC1 isoforms differ in their affinity for chromatin, molecular interactions and regulation by phosphorylation. J. Cell Sci. 120: 3436-3445 [Abstract] [Full Text]  


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