Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 521, Issue 4, Pages 1010-1016Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2019.11.039
Keywords
Smad2; Glycosylation; Transforming growth factor-beta 1
Categories
Funding
- Oves Minnesfond
- QNRF [NPRP9-453-3-089]
- Qatar University [QUCG-CMED-2018/2019-2]
- JSPS KAKENHI [JP 26461707]
Ask authors/readers for more resources
Smad2 is a crucial component of intracellular signaling by transforming growth factor-beta (TGF beta ). Here we describe that Smad2 is glycosylated, which is a novel for Smad2 post-translational modification. We showed that the Smad2 glycosylation was inhibited upon treatment of cells with 17 beta-estradiol, and was enhanced in cells in a dense culture as compared to cells in a sparse culture. The Smad2 glycosylation was not dependent on the C-terminal phosphorylation of Smad2, and was not affected by TGF beta 1 treatment of the cells. Smad2 was glycosylated at multiple sites, and one of the predicted sites is Serine110. Thus, Smad2 is glycosylated, and this post-translational modification was modulated by 17 beta-estradiol but not by TGF beta 1. (C) 2019 Elsevier Inc. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available