Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2020 Jun 25;12(2):89–106. doi: 10.1007/s13238-020-00741-7

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Glycosylation of TGF-β receptors and co-receptors. TGF-β receptors and co-receptors can be highly glycosylated with N-linked and O-linked glycans. Core fucosylation of TβRII and TβRI are required for their successful localization at the cell surface . In addition, the β1,6 branching structures of TβRII reinforces TGF-β signaling by inhibiting the endocytosis of TGF-β receptors. Lewis^X (sLe^X) and sialyl-Lewis^A (sLe^A) modified on TβRI are necessary for its activation. Betaglycan is composed of a core protein with covalently linked glycosaminoglycans (GAG) chains. Glycosphingolipids (GSLs), together with cholesterol, form microdomains, which are referred to as lipid rafts. The GSLs in these microdomains might paly a role in membrane trafficking of TGF-β receptors and signal transduction.