Dimerization of small integral membrane protein 1 promotes cell surface presentation of the Vel blood group epitope
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/e1705ba0-ae35-48f9-bf0f-e215e107b305
- author
- Kelley, Liam P.
; Nylander, Anja
LU
; Arnaud, Lionel ; Schmoker, Anna M. ; St. Clair, Riley M. ; Gleason, Lindsey A. ; Souza, Jessica M. ; Storry, Jill R. LU ; Olsson, Martin L. LU
and Ballif, Bryan A.
- organization
- publishing date
- 2020-04
- 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}}, }