Glycosylation is a novel TGF?1-independent post-translational modification of Smad2
| Author | Gotoh, Takaya |
| Author | Iwahana, Hiroyuki |
| Author | Kannan, Surya |
| Author | Marei, Reham Ghazal |
| Author | Mousa, Hanaa |
| Author | Elgamal, Mahmoud |
| Author | Souchelnytskyi, Serhiy |
| Available date | 2020-08-18T08:34:45Z |
| Publication Date | 2019 |
| Publication Name | Biochemical and Biophysical Research Communications |
| Resource | Scopus |
| ISSN | 0006291X |
| Abstract | Smad2 is a crucial component of intracellular signaling by transforming growth factor-? (TGF?). 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?-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?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?-estradiol but not by TGF?1. - 2019 Elsevier Inc. |
| Sponsor | The authors are grateful to the Oves Minnesfond for support and encouragement. Gift of the ARE-luc reporter and FAST1 construct from Dr. Vogelstein is acknowledged. This work was supported in part by QNRF (grant number NPRP9-453-3-089 ) and Qatar University (grant number QUCG-CMED-2018/2019-2 ) grants to S.S., and by� JSPS KAKENHI grant number JP 26461707 to T.G. Appendix A |
| Language | en |
| Publisher | Elsevier B.V. |
| Subject | Glycosylation Smad2 Transforming growth factor-?1 |
| Type | Article |
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