Genetic regulation of post-translational modification of two distinct proteins

Post-translational modifications diversify protein functions and dynamically coordinate their signalling networks, influencing most aspects of cell physiology. Nevertheless, their genetic regulation or influence on complex traits is not fully understood. Here, we compare the genetic regulation of th...

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Vydané v:Nature communications Ročník 13; číslo 1; s. 1586 - 13
Hlavní autori: Landini, Arianna, Trbojević-Akmačić, Irena, Navarro, Pau, Tsepilov, Yakov A., Sharapov, Sodbo Z., Vučković, Frano, Polašek, Ozren, Hayward, Caroline, Petrović, Tea, Vilaj, Marija, Aulchenko, Yurii S., Lauc, Gordan, Wilson, James F., Klarić, Lucija
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: London Nature Publishing Group UK 24.03.2022
Nature Publishing Group
Nature Portfolio
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45/43
49/47
631/208/205/2138
631/337/458/1524
Association analysis
Genes
Genetic diversity
Genome-Wide Association Study
Genomes
Glycosylation
Humanities and Social Sciences
IgG antibody
Immunoglobulin G
Immunoglobulin G - metabolism
multidisciplinary
Post-translation
Protein Processing, Post-Translational
Proteins
Science
Science (multidisciplinary)
Transferrin
Transferrin - genetics
Transferrin - metabolism
Transferrins
Translation
ISSN:2041-1723, 2041-1723
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Shrnutí:Post-translational modifications diversify protein functions and dynamically coordinate their signalling networks, influencing most aspects of cell physiology. Nevertheless, their genetic regulation or influence on complex traits is not fully understood. Here, we compare the genetic regulation of the same PTM of two proteins – glycosylation of transferrin and immunoglobulin G (IgG). By performing genome-wide association analysis of transferrin glycosylation, we identify 10 significantly associated loci, 9 of which were not reported previously. Comparing these with IgG glycosylation-associated genes, we note protein-specific associations with genes encoding glycosylation enzymes (transferrin - MGAT5 , ST3GAL4 , B3GAT1 ; IgG - MGAT3 , ST6GAL1 ), as well as shared associations ( FUT6 , FUT8 ). Colocalisation analyses of the latter suggest that different causal variants in the FUT genes regulate fucosylation of the two proteins. Glycosylation of these proteins is thus genetically regulated by both shared and protein-specific mechanisms. Post-translational modifications are known to diversify protein functions, but the effect of genetic variation on the modifications is not well known. Here, the authors find both shared and protein-specific genetic mechanisms regulating the glycosylation of two different proteins.
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ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-022-29189-5