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Novel post-translational modifications of Smad2 identified by mass spectrometry
Karolinska University Hospital. (Department of Oncology-Pathology)
Karolinska University Hospital. (Department of Oncology-Pathology)
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry, Analytical Chemistry.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
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2008 (English)In: Central European Journal of Biology, ISSN 1895-104X, E-ISSN 1644-3632, Vol. 3, no 4, 359-370 p.Article in journal (Refereed) Published
Abstract [en]

Smad2 is a crucial component of transforming growth factor-b (TGFb) signaling, and is involved in the regulation of cell proliferation,death and differentiation. Phosphorylation, ubiquitylation and acetylation of Smad2 have been found to regulate its activity. We usedmass spectrometry to search for novel post-translational modifications (PTMs) of Smad2. Peptide mass fingerprinting (PMF) indicatedthat Smad2 can be acetylated, methylated, citrullinated, phosphorylated and palmitoylated. Sequencing of selected peptides validatedmethylation at Gly122 and hydroxylation at Trp18 of Smad2. We also observed a novel, so far unidentified modification at Tyr128 andTyr151. Our observations open for further exploration of biological importance of the detected PTMs.

Place, publisher, year, edition, pages
2008. Vol. 3, no 4, 359-370 p.
Keyword [en]
Smad2, mass spectrometry, post-translational modifications
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-99985DOI: 10.2478/s11535-008-0045-2ISI: 000259696700004OAI: oai:DiVA.org:uu-99985DiVA: diva2:209107
Swedish Research Council, 629-2002-6821Swedish Research Council, 342-2004-3944Swedish Research Council, 621-2005-5379
Available from: 2009-03-23 Created: 2009-03-23 Last updated: 2015-08-18Bibliographically approved

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Bergquist, Jonas
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Analytical ChemistryLudwig Institute for Cancer Research
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