Proteomics

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Molecular mechanism of distinct chemokine engagement and functional divergence of the human Duffy antigen receptor

ABSTRACT: The Duffy antigen receptor, also known as FY glycoprotein or CD234, is a seven transmembrane (7TM) protein expressed primarily at the surface of red blood cells, and it displays strikingly promiscuous binding to multiple pro- and anti-inflammatory chemokines. Here, we comprehensively profile transducer-coupling for this receptor including G-proteins, GRKs, and β-arrestins to unequivocally establish its dramatic functional divergence, and discover potential non-canonical signaling pathways using a global phosphoproteomics analysis. we present a comprehensive profiling of transducer-coupling for this receptor using cell-based assays, and a global phosphoproteomics screen to identify novel, non-canonical downstream signaling pathways. We prepared samples under unstimulated and CCL7-stimulated conditions, generated proteolytic fragments by trypsin digestion, enriched for phosphorylated peptides using TiO2 beads, and then identified the phosphorylated peptides using liquid chromatography-tandem MS (LC-MS/MS).

INSTRUMENT(S): Orbitrap Exploris 240

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: gagan jhingan  

LAB HEAD: Dr. Arun

PROVIDER: PXD044876 | Pride | 2024-10-17

REPOSITORIES: Pride

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Publications

The Duffy antigen receptor is a seven-transmembrane (7TM) protein expressed primarily at the surface of red blood cells and displays strikingly promiscuous binding to multiple inflammatory and homeostatic chemokines. It serves as the basis of the Duffy blood group system in humans and also acts as the primary attachment site for malarial parasite Plasmodium vivax and pore-forming toxins secreted by Staphylococcus aureus. Here, we comprehensively profile transducer coupling of this receptor, disc  ...[more]

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