Novel post-translational modifications of Smad2 identified by mass spectrometry
Abstract: Smad2 is a crucial component of transforming growth factor-β (TGFβ) 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 used mass spectrometry to search for novel post-translational modifications (PTMs) of Smad2. Peptide mass fingerprinting (PMF) indicated that Smad2 can be acetylated, methylated, citrullinated, phosphorylated and palmitoylated. Sequencing of selected peptides validated methylation at Gly122 and hydroxylation at Trp18 of Smad2. We also observed a novel, so far unidentified modification at Tyr128 and Tyr151. Our observations open for further exploration of biological importance of the detected PTMs.
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
Novel post-translational modifications of Smad2 identified by mass spectrometry ; volume:3 ; number:4 ; year:2008 ; pages:359-370 ; extent:12
Open life sciences ; 3, Heft 4 (2008), 359-370 (gesamt 12)
- Creator
-
Bhaskaran, Nimesh
Iwahana, Hiroyuki
Bergquist, Jonas
Hellman, Ulf
Souchelnytskyi, Serhiy
- DOI
-
10.2478/s11535-008-0045-2
- URN
-
urn:nbn:de:101:1-2409201811025.164744342524
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:23 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Bhaskaran, Nimesh
- Iwahana, Hiroyuki
- Bergquist, Jonas
- Hellman, Ulf
- Souchelnytskyi, Serhiy