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MBC in Press, published online ahead of print July 29, 2005
Mol. Biol. Cell 10.1091/mbc.E05-03-0257

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Submitted on March 28, 2005
Revised on July 7, 2005
Accepted on July 18, 2005

Phosphoproteome Profiling of Transforming Growth Factor-{beta} Signaling: Abrogation of TGF{beta}1-dependent Phosphorylation of TFII-I Enhances Cooperation of TFII-I and Smad3 in Transcription

Taras Stasyk,*{dagger} Anna Dubrovska,*{dagger} Marta Lomnytska,*{ddagger} Ihor Yakymovych,* Christer Wernstedt,* Carl-Henrik Heldin,* Ulf Hellman,* and Serhiy Souchelnytskyi*

*Ludwig Institute for Cancer Research, Uppsala University, SE-751 24 Uppsala, Sweden; {ddagger}Department of Oncology and Medical Radiology, Lviv National Medical University, UA-79031 Lviv, Ukraine

Monitoring Editor: Richard Assoian

Transforming growth factor-{beta} (TGF{beta}) signaling involves activation of a number of signaling pathways, several of which are controlled by phosphorylation events. Here we describe a phosphoproteome profiling of MCF-7 human breast epithelial cells treated with TGF{beta}1. We identified 32 proteins which change their phosphorylation upon treatment with TGF{beta}1; 26 of these proteins are novel targets of TGF{beta}1. We show that Smad2 and Smad3 have different effects on the dynamics of TGF{beta}1-induced protein phosphorylation. The identified proteins belong to nine functional groups, e.g., proteins regulating RNA processing, cytoskeletal rearrangements and proteasomal degradation. To evaluate the proteomics findings, we explored the functional importance of TGF{beta}1-dependent phosphorylation of one of the targets, i.e., transcription factor-II-I (TFII-I). We confirmed that TGF{beta}1 stimulated TFII-I phosphorylation at serine residues 371 and 743. Abrogation of the phosphorylation by replacement of Ser371 and Ser743 with alanine residues resulted in enhanced complex formation between TFII-I and Smad3, and enhanced cooperation between TFII-I and Smad3 in transcriptional regulation, as evaluated by a microarray-based measurement of expression of endogenous cyclin D2, cyclin D3 and E2F2 genes, and by a luciferase reporter assay. Thus, TGF{beta}1-dependent phosphorylation of TFII-I may modulate TGF{beta} signaling at the transcriptional level.

{dagger}These authors contributed equally to this work.

Address correspondence to: Serhiy Souchelnytskyi (serhiy.souchelnytskyi{at}licr.uu.se)




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