ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2015
The atypical N-glycosylation motif, Asn-Cys-Cys, in human GPR109A is required for normal cell surface expression and intracellular signaling.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 15 citations in OpenAlex.
- Lipid-Based Delivery Systems for Therapeutic Glycoproteins: Current Advances, Challenges, and Future Perspectives.Pharmaceutics · 2026Review
- Orthosteric and allosteric modulation of human HCAR2 signaling complex.Nature communications · 2023Article
- Hyaluronic acid-GPRC5C signalling promotes dormancy in haematopoietic stem cells.Nature cell biology · 2022Article
- Rare and potentially pathogenic variants in hydroxycarboxylic acid receptor genes identified in breast cancer cases.BMC medical genomics · 2021Article
- Site-Specific N- and O-Glycosylation Analysis of Human Plasma Fibronectin.Frontiers in chemistry · 2021Article
- The Gα12/13-coupled receptor LPA4 limits proper adipose tissue expansion and remodeling in diet-induced obesity.JCI insight · 2018Article
- Refined topology model of the STT3/Stt3 protein subunit of the oligosaccharyltransferase complex.The Journal of biological chemistry · 2017Article
- Proteoform Profile Mapping of the Human Serum Complement Component C9 Revealing Unexpected New Features of N-, O-, and C-Glycosylation.Analytical chemistry · 2017Article
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5 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Asparagine-linked glycosylation (N-glycosylation) is necessary for the proper folding of secreted and membrane proteins, including GPCRs. Thus, many GPCRs possess the N-glycosylation motif Asn-X-Ser/Thr at their N-termini and/or extracellular loops. We found that human GPR109A (hGPR109A) has an N-glycosylation site at Asn(17) in the N-terminal atypical motif, Asn(17)-Cys(18)-Cys(19). Why does hGPR109A require the atypical motif, rather than the typical sequence? Here we show that Asn(17)-Cys(18)-Cys(19) sequence of hGPR109A possesses 2 biologic roles. First, Asn(17)-X-Cys(19) contributed to hGPR109A N-glycosylation by acting as an atypical motif. This modification is required for the normal surface expression of hGPR109A, as evidenced by the reduced surface expression of the nonglycosylated mutants, hGPR109A/N17A, and the finding that hGPR109A/C19S and hGPR109A/C19T, which are N-glycosylated at Asn(17), exhibited expression similar to the wild-type receptor. Second, the X-Cys(18)-Cys(19) dicysteine is indispensable for hGPR109A function. Substitution of Cys(18) or Cys(19) residue to Ala impaired Gi-mediated signaling via hGPR109A. We propose the disulfide bond formations of these residues with other Cys existed in the extracellular loops for the proper folding. Together, these results suggest that the atypical motif Asn(17)-Cys(18)-Cys(19) is crucial for the normal surface trafficking and function of hGPR109A.
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