ArticleGlycosylation of the GLP-1 receptor is a prerequisite for regular receptor function
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Effects of Glucagon-like peptide 1 (GLP-1) analogs in the hippocampus
2022, Vitamins and HormonesCitation Excerpt :The GLP-1 receptor (GLP-1R) is 463 amino acids long. It contains seven transmembrane domains with the presence of an amino-terminal hydrophobic region following by a hydrophilic domain of 120 amino acids, which contains three N-linked glycosylation sites, that is essential for the receptor function, standard folding, and trafficking to the cell surface (Chen, Miller, & Dong, 2010; Göke, Just, Lankat-Buttgereit, & Göke, 1994; Thorens, 1992). The activation of GLP-1R stimulates cAMP formation via the stimulatory G protein (Gs) signaling, increases intracellular Ca2 + via the Gq/11 pathway, and promotes ERK1/2 signaling via recruitment of β-arrestin (Mayo et al., 2003; Müller et al., 2019).
Targeting the glucagon receptor family for diabetes and obesity therapy
2012, Pharmacology and TherapeuticsCitation Excerpt :Crystal structure analysis of the GLP-1R in complex with exendin(9–39) revealed that the hydrophobic binding site of the GLP-1R is composed of discontinuous segments of α-helix in the N-terminus and a loop between two antiparallel β-strands (Runge et al., 2008). Both glycosylation and palmitoylation of the GLP-1R modulate its function in vitro (Goke et al., 1994; Vazquez et al., 2005). However, it is unknown if these posttranslational modifications affect the biological function of the GLP-1R in vivo.
Structural Basis for Ligand Recognition of Incretin Receptors
2010, Vitamins and HormonesCitation Excerpt :The ECD contains three disulfide bridges and three potential asparagine (N)-linked glycosylation sites (Thorens, 1992). Inhibition of the glycosylation process with tunicamycin reduced the number of GLP-1 binding sites, indicating that glycosylation of the GLP-1R ECD is important for receptor expression at the cell surface but not for ligand binding (Göke et al., 1994). The isolated ECD of the GLP-1R can be expressed recombinantly in Escherichia coli inclusion bodies and refolded to form a functional receptor domain (Bazarsuren et al., 2002; López de et al., 2003; Runge et al., 2007).
Modulation of TSHR signaling by posttranslational modifications
2007, Trends in Endocrinology and MetabolismCitation Excerpt :This ensures that only correctly folded proteins are transported to the Golgi apparatus. For most receptors of the 7TMR superfamily, impaired glycosylation is associated with decreased cell-surface expression of normally active receptors [38–45]. However, the inability of the TSHR to bind TSH in non-mammalian expression systems reflects an important role of these complex carbohydrates in the correct folding of the TSHR ectodomain.
Mechanisms of action of glucagon-like peptide 1 in the pancreas
2007, Pharmacology and TherapeuticsCitation Excerpt :Treatment resulted in a concentration-dependent reduction in association of the cells with GLP-1 due to a decrease in the number GLP-1 binding sites in the membrane. The reduction in GLP-1R expression at the cell membrane was detected using radiolabeled [125I]GLP-1 and was not a consequence of an inhibition of transcription as mRNA levels in treated cells did not differ (Goke et al., 1994). There was also a reduction in cAMP production and together these results indicate that glycosylation of GLP-1R is necessary for correct insertion into the cell membrane and function.
Glucagon-like peptide receptor
2007, xPharm: The Comprehensive Pharmacology Reference