Nuclear Localization Signal and Protein Context both Mediate Importin α Specificity of Nuclear Import Substrates

Author:

Friedrich Beate1,Quensel Christina1,Sommer Thomas1,Hartmann Enno2,Köhler Matthias134

Affiliation:

1. The Max Delbrueck Center for Molecular Medicine, Robert Roessle Str. 10, 13125 Berlin, Germany

2. Institute of Biology, Center of Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

3. Nephrology Section, Franz Volhard Clinic, HELIOS Klinikum Berlin, Wiltbergstr. 50, 13125 Berlin, Germany

4. Center for Nephrology and Hypertension, Ostsee Clinic and Reha Clinic Damp, Seute-Deern-Ring 30, 24351 Damp, Germany

Abstract

ABSTRACT The “classical” nuclear protein import pathway depends on importin α and importin β. Importin α binds nuclear localization signal (NLS)-bearing proteins and functions as an adapter to access the importin β-dependent import pathway. In humans, only one importin β is known to interact with importin α, while six α importins have been described. Various experimental approaches provided evidence that several substrates are transported specifically by particular α importins. Whether the NLS is sufficient to mediate importin α 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 α3, 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 α binding and transport.

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

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