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Published 9 May 2005. doi:10.1083/jcb.200411169
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 3, 415-424
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Article

Promotion of importin {alpha}–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3



Christian Faul1,2,4, Stefan Hüttelmaier2, Jun Oh1, Virginie Hachet3, Robert H. Singer2, and Peter Mundel1,2,4

1 Department of Medicine, Albert Einstein College of Medicine, Bronx, NY 10461
2 Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461
3 European Molecular Biology Laboratory, 69117 Heidelberg, Germany
4 Department of Medicine, Mount Sinai School of Medicine, New York, NY 10029

Correspondence to Peter Mundel: peter.mundel{at}mssm.edu

14-3-3 proteins are phosphoserine/threonine-binding proteins that play important roles in many regulatory processes, including intracellular protein targeting. 14-3-3 proteins can anchor target proteins in the cytoplasm and in the nucleus or can mediate their nuclear export. So far, no role for 14-3-3 in mediating nuclear import has been described. There is also mounting evidence that nuclear import is regulated by the phosphorylation of cargo proteins, but the underlying mechanism remains elusive. Myopodin is a dual-compartment, actin-bundling protein that functions as a tumor suppressor in human bladder cancer. In muscle cells, myopodin redistributes between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced fashion. We show that importin {alpha} binding and the subsequent nuclear import of myopodin are regulated by the serine/threonine phosphorylation-dependent binding of myopodin to 14-3-3. These results establish a novel paradigm for the promotion of nuclear import by 14-3-3 binding. They provide a molecular explanation for the phosphorylation-dependent nuclear import of nuclear localization signal-containing cargo proteins.

Abbreviations used in this paper: {lambda}-PPase, {lambda} protein phosphatase; IP, immunoprecipitation; LMB, leptomycin B; NLS, nuclear localization signal; pGEX, glutathione S-transferase fusion vector.


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