Signalling and transport converge

Cesari, Francesca

doi:10.1038/nrm2386

Research Highlight
Published: April 2008

Nuclear transport

Signalling and transport converge

Francesca Cesari

Nature Reviews Molecular Cell Biology volume 9, page 265 (2008)Cite this article

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Using a two-hybrid screen to identify new targets of the ribosomal S6 kinase (RSK), a downstream effector of the Ras–ERK signalling pathway, Blenis and colleagues identified Ran-binding protein-3 (RanBP3), a regulator of Ran GTPase, which coordinates the nucleocytoplasmic transport of many proteins and RNAs. The authors showed that activated RSK phosphorylates residue Ser58 of RanBP3 in cells. Ser58 is also phosphorylated by activated AKT/PKB, a kinase of the PI3K signalling pathway, but not by other kinases.

So, what is the effect of RanBP3 phosphorylation in vivo? To address this question, Blenis and co-workers expressed endogenous levels of RanBP3 and a GTP-bound Ran mutant that associates weakly with RanBP3, in cells lacking the two endogenous proteins. Upon RanBP3 phosphorylation, the interaction between the two proteins increases, which suggests that the serum-induced Ser58 phosphorylation increases the affinity of RanBP3 for Ran. Indeed, a RanBP3 mutant that cannot be phosphorylated (S58A) did not show an increased interaction with Ran.

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ORIGINAL RESEARCH PAPER

Yoon, S-O. et al. Ran-binding protein 3 phosphorylation links the Ras and PI3-kinase pathways to nucleocytoplasmic transport. Mol. Cell 29, 362–375 (2008)
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