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Dimerization of small integral membrane protein 1 promotes cell surface presentation of the Vel blood group epitope

Kelley, Liam P. ; Nylander, Anja LU orcid ; Arnaud, Lionel ; Schmoker, Anna M. ; St. Clair, Riley M. ; Gleason, Lindsey A. ; Souza, Jessica M. ; Storry, Jill R. LU ; Olsson, Martin L. LU orcid and Ballif, Bryan A. (2020) In FEBS Letters 594(8). p.1261-1270
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.

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author
; ; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
disulfide bond, GxxxG, SMIM1, transfusion medicine, Vel blood group system
in
FEBS Letters
volume
594
issue
8
pages
10 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:85078602210
  • pmid:31879955
ISSN
0014-5793
DOI
10.1002/1873-3468.13726
project
Further investigation into the structure and function of SMIM1, a newly discovered erythroid transmembrane protein
language
English
LU publication?
yes
id
e1705ba0-ae35-48f9-bf0f-e215e107b305
date added to LUP
2020-02-10 15:50:27
date last changed
2024-06-26 11:09:30
@article{e1705ba0-ae35-48f9-bf0f-e215e107b305,
  abstract     = {{<p>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.</p>}},
  author       = {{Kelley, Liam P. and Nylander, Anja and Arnaud, Lionel and Schmoker, Anna M. and St. Clair, Riley M. and Gleason, Lindsey A. and Souza, Jessica M. and Storry, Jill R. and Olsson, Martin L. and Ballif, Bryan A.}},
  issn         = {{0014-5793}},
  keywords     = {{disulfide bond; GxxxG; SMIM1; transfusion medicine; Vel blood group system}},
  language     = {{eng}},
  number       = {{8}},
  pages        = {{1261--1270}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{FEBS Letters}},
  title        = {{Dimerization of small integral membrane protein 1 promotes cell surface presentation of the Vel blood group epitope}},
  url          = {{http://dx.doi.org/10.1002/1873-3468.13726}},
  doi          = {{10.1002/1873-3468.13726}},
  volume       = {{594}},
  year         = {{2020}},
}