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Proteomics-based identification of proteins interacting with Smad3: SREBP-2 forms a complex with Smad3 and inhibits its transcriptional activity
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
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2004 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 577, no 1-2, 93-100 p.Article in journal (Refereed) Published
Abstract [en]

Smad3 is an important component of transforming growth factor-beta (TGFbeta) intracellular signalling. To identify novel interacting proteins of Smad3, we performed pull-down assays with Smad3 constructs fused to glutathione-S-transferase. Proteins which formed complexes with these constructs were analyzed by two-dimensional gel electrophoresis, and were identified by matrix-assisted laser desorption-ionization time-of-flight mass spectrometry. We identified 14 proteins interacting with the Smad3 construct lacking the N-terminal Mad homology domain 1 (MH1), and 12 proteins interacting with the construct lacking the C-terminal MH2 domain. Proteins involved in signalling processes, in metabolism regulation, novel proteins, and components of cytoskeleton form four groups of interacting proteins. Interactions of AGP7, sex-determining region Y protein, actin beta and sterol regulatory element binding protein-2 (SREBP-2) proteins with Smad3 constructs were confirmed by immunoblotting with specific antibodies. Interaction of Smad3 with SREBP-2 was also confirmed by co-immunoprecipitation of myc-Smad3 and Flag-SREBP-2 upon expression in mammalian cells. We found that SREBP-2 inhibited the transcriptional activity of Smad3 in luciferase reporter assays.

Place, publisher, year, edition, pages
2004. Vol. 577, no 1-2, 93-100 p.
Keyword [en]
Animals, Cell Line, DNA-Binding Proteins/*metabolism, Electrophoresis; Gel; Two-Dimensional, Humans, Protein Binding, Proteome, Research Support; Non-U.S. Gov't, Spectrometry; Mass; Matrix-Assisted Laser Desorption-Ionization, Trans-Activators/*metabolism, Transcription Factors/*metabolism, Transcription; Genetic
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Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-72965DOI: 10.1016/j.febslet.2004.09.069PubMedID: 15527767OAI: oai:DiVA.org:uu-72965DiVA: diva2:100876
Available from: 2005-05-31 Created: 2005-05-31 Last updated: 2017-12-14Bibliographically approved

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Grimsby, SusanneDubrovska, AnnaHellman, UlfSouchelnytskyi, Serhiy

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