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Published online
doi:10.1083/jcb.200703106
The Journal of Cell Biology, Vol. 178, No. 6, 981-994
The Rockefeller University Press, 0021-9525 $30.00
© Xu et al.
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Article

Msk is required for nuclear import of TGF-ß/BMP-activated Smads



Lan Xu1, Xiaohao Yao1, Xiaochu Chen1, Peiyuan Lu1, Biliang Zhang2, and Y. Tony Ip1

1 Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605
2 Guangzhou Institute of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510663 China

Correspondence to Lan Xu: lan.xu{at}umassmed.edu

Nuclear translocation of Smad proteins is a critical step in signal transduction of transforming growth factor ß (TGF-ß) and bone morphogenetic proteins (BMPs). Using nuclear accumulation of the Drosophila Smad Mothers against Decapentaplegic (Mad) as the readout, we carried out a whole-genome RNAi screening in Drosophila cells. The screen identified moleskin (msk) as important for the nuclear import of phosphorylated Mad. Genetic evidence in the developing eye imaginal discs also demonstrates the critical functions of msk in regulating phospho-Mad. Moreover, knockdown of importin 7 and 8 (Imp7 and 8), the mammalian orthologues of Msk, markedly impaired nuclear accumulation of Smad1 in response to BMP2 and of Smad2/3 in response to TGF-ß. Biochemical studies further suggest that Smads are novel nuclear import substrates of Imp7 and 8. We have thus identified new evolutionarily conserved proteins that are important in the signal transduction of TGF-ß and BMP into the nucleus.

Abbreviations used in this paper: BMP, bone morphogenetic protein; dad, daughters against decapentaplegic; Dpp, Decapentaplegic; Mad, Mothers against decapentaplegic; Msk, Moleskin; Tkv, Thickvein.


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