GOTOH Takaya   Faculty of Sports and Health Science Department of Health Science   Professor

■ Title   Glyosylation is a novel TGFb-independent post-tranaslational modification of Smasd2

■ Outline   Smad2 is a crucial component of intracellular signaling by transforming growth factor-b (TGFb). 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 17b-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 TGFb1 treatment of the cells. Smad2 was glycosylated at multiple sites, and one of the predicted sites is Seine 110. Thus, Smad2 is glycosylated, and this post-translational modification was modulated by 17b-estradiol but not by TGFb1.   ◎Gotoh T, Iwahana H, Kannan S, Marei RG, Mousa H, Elgamal M, Souchelnytskyi S.   Collaboration   Biochem Biophys Res Commun.   4(521),pp.1010   2020/01

Copyright(C) 2011 Daito Bunka University, All rights reserved.