Publication Date:
2019
Description:
Abstract
The Vel blood group antigen is carried on the short extracellular segment of the 78 amino acid long, type II transmembrane protein SMIM1 of unknown function. Here using biochemical analysis and flow cytometry of cells expressing wild type and mutant alleles of SMIM1, we demonstrate that dimerization of SMIM1 promotes cell surface display of the Vel epitope. We show that SMIM1 dimerization is mediated both by an extracellular Cys77‐dependent, homomeric disulfide linkage and via a GxxxG helix‐helix interaction motif in the transmembrane domain. These results provide important context for the observed variability in reactivity patterns of clinically important anti‐Vel identified in patient sera.
Print ISSN:
0014-5793
Electronic ISSN:
1873-3468
Topics:
Biology
,
Chemistry and Pharmacology
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