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

This object is provided by:
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

Other Objects (12)