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Glycosylation is a novel TGFβ1-independent post-translational modification of Smad2.

Abstract：

:Smad2 is a crucial component of intracellular signaling by transforming growth factor-β (TGFβ). 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 17β-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 TGFβ1 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 17β-estradiol but not by TGFβ1.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Gotoh T,Iwahana H,Kannan S,Marei RG,Mousa H,Elgamal M,Souchelnytskyi S

doi

10.1016/j.bbrc.2019.11.039

subject

Has Abstract

pub_date

2020-01-22 00:00:00

pages

1010-1016

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(19)32159-X

journal_volume

521

pub_type

杂志文章

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