Figure 1 | Scientific Reports

Figure 1

From: Inhibition of post-translational N-glycosylation by HRD1 that controls the fate of ABCG5/8 transporter

Figure 1

Determination of N-linked glycosylation sites in human ABCG5 and ABCG8.

(a) Putative asparagine residues to be N-glycosylated in human ABCG5 protein. (b) Steady-state expression of monomeric Myc-tagged WT-, N584Q-, N591Q- and N584Q-/N591Q-ABCG5 was analyzed by immunoblotting. (c) Endo H (500 U) and PNGase F (500 U) sensitivity of Myc-tagged WT-, N584Q-, N591Q- and N584Q-/N591Q-ABCG5 proteins shown in (b). (d) Putative asparagine residue to be N-glycosylated in human ABCG8 protein. (e) Endo H and PNGase F sensitivity of HA-tagged WT- or N619Q-ABCG8 proteins. (f) Schematic flow of intracellular trafficking pathway of ABCG5 and ABCG8 proteins. Complex-glycosylated, high-mannose, di-glycosylated, mono-glycosylated and non-glycosylated forms of ABCG5 and ABCG8 proteins are represented as C-G, HM, Di-G, Mono-G and Non-G, respectively. Gels have been cropped for clarity; full-length gels of Figure 1b, 1c and 1e are presented in Supplementary Figure S4.

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