- AutorIn
- Liane Fischer
- Caroline Wilde
- Torsten Schöneberg
- Ines Liebscher
- Titel
- Functional relevance of naturally occurring mutations in adhesion G protein-coupled receptor ADGRD1 (GPR133)
- Zitierfähige Url:
- https://nbn-resolving.org/urn:nbn:de:bsz:15-qucosa-208803
- Quellenangabe
- BMC Genomics (2016) 17:609 DOI 10.1186/s12864-016-2937-2
- Erstveröffentlichung
- 2016
- Abstract (EN)
- Background: A large number of human inherited and acquired diseases and phenotypes are caused by mutations in G protein-coupled receptors (GPCR). Genome-wide association studies (GWAS) have shown that variations in the ADGRD1 (GPR133) locus are linked with differences in metabolism, human height and heart frequency. ADGRD1 is a Gs protein-coupled receptor belonging to the class of adhesion GPCRs. Results: Analysis of more than 1000 sequenced human genomes revealed approximately 9000 single nucleotide polymorphisms (SNPs) in the human ADGRD1 as listed in public data bases. Approximately 2.4 % of these SNPs are located in exons resulting in 129 non-synonymous SNPs (nsSNPs) at 119 positions of ADGRD1. However, the functional relevance of those variants is unknown. In-depth characterization of these amino acid changes revealed several nsSNPs (A448D, Q600stop, C632fs [frame shift], A761E, N795K) causing full or partial loss of receptor function, while one nsSNP (F383S) significantly increased basal activity of ADGRD1. Conclusion: Our results show that a broad spectrum of functionally relevant ADGRD1 variants is present in the human population which may cause clinically relevant phenotypes, while being compatible with life when heterozygous.
- Andere Ausgabe
- Link zur Originalpublikation in der Zeitschrift BMC Genomics
Link: http://dx.doi.org/10.1186/s12864-016-2937-2 - Freie Schlagwörter (DE)
- G-Protein-gekoppelte Rezeptor 133, ADGRD1, Adhäsions-G-Protein-gekoppelte Rezeptor, Mutation, Einzelnukleotid-Polymorphismus, Datenbank
- Freie Schlagwörter (EN)
- GPR133, ADGRD1, Adhesion GPCR, Mutations, SNP, Database
- Klassifikation (DDC)
- 572
- Herausgeber (Institution)
- Universität Leipzig
- Verlag
- BioMed Central, London
- URN Qucosa
- urn:nbn:de:bsz:15-qucosa-208803
- Veröffentlichungsdatum Qucosa
- 18.08.2016
- Dokumenttyp
- Artikel
- Sprache des Dokumentes
- Englisch