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M700636200v1
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Papers In Press, published online ahead of print April 23, 2007
J. Biol. Chem, 10.1074/jbc.M700636200
Submitted on January 23, 2007
Revised on April 23, 2007
Accepted on April 23, 2007

Activation of Mps1 promotes TGF-beta independent Smad signaling

Songcheng Zhu, Wei Wang, David C. Clarke, and Xuedong Liu

Chemistry and Biochemistry, University of Colorado-Boulder, Boulder, CO 80309

Corresponding Author: liux{at}colorado.edu

The primary intracellular mediators of TGF-ß signaling are the Smad proteins. Phosphorylation of R-Smad at the carboxyl terminal SSXS motif by the activated TGF-ß type I receptor kinase triggers a conformation change in R-Smad and facilitates complex formation between R-Smad and Smad4, which shuttle into the nucleus where they interact with DNA and other transcription factors to regulate gene expression. In an attempt to identify proteins interacting with activated Smad signaling complex, we discovered that Mps1, a protein kinase that plays important roles in normal mitotic progression and mitotic checkpoint signaling, co-purifies with this complex. We demonstrated that Smad2 and Smad3 but not Smad4 are substrates of Mps1 in vitro and in vivo. Mps1 phosphorylates Smad2 and Smad3 at the SSXS motif in their carboxyl terminal regions in vitro and in vivo. Disruption of microtubule networks by nocodazole activates Mps1 and promotes TGF-ß-independent activation of Smad signaling. We found that Mps1 is involved in turning on Smad signaling by phosphorylating R-Smads. Our results reveal a novel functional link between Mps1 and Smads in a non-canonical Smad signaling pathway.


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