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Dimerization of sma...
Dimerization of small integral membrane protein 1 promotes cell surface presentation of the Vel blood group epitope
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- Kelley, Liam P. (author)
- University of Vermont
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- Nylander, Anja (author)
- Lund University,Lunds universitet,Avdelningen för hematologi och transfusionsmedicin,Institutionen för laboratoriemedicin,Medicinska fakulteten,Transfusionsmedicin,Forskargrupper vid Lunds universitet,Division of Hematology and Transfusion Medicine,Department of Laboratory Medicine,Faculty of Medicine,Transfusion Medicine,Lund University Research Groups,Central Hospital Kristianstad
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- Arnaud, Lionel (author)
- University of Vermont
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- Schmoker, Anna M. (author)
- University of Vermont
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- St. Clair, Riley M. (author)
- University of Vermont
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- Gleason, Lindsey A. (author)
- University of Vermont
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- Souza, Jessica M. (author)
- University of Vermont
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- Storry, Jill R. (author)
- Lund University,Lunds universitet,Avdelningen för hematologi och transfusionsmedicin,Institutionen för laboratoriemedicin,Medicinska fakulteten,Transfusionsmedicin,Forskargrupper vid Lunds universitet,Division of Hematology and Transfusion Medicine,Department of Laboratory Medicine,Faculty of Medicine,Transfusion Medicine,Lund University Research Groups,Region Skåne
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- Olsson, Martin L. (author)
- Lund University,Lunds universitet,Avdelningen för hematologi och transfusionsmedicin,Institutionen för laboratoriemedicin,Medicinska fakulteten,Transfusionsmedicin,Forskargrupper vid Lunds universitet,Division of Hematology and Transfusion Medicine,Department of Laboratory Medicine,Faculty of Medicine,Transfusion Medicine,Lund University Research Groups,Region Skåne
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- Ballif, Bryan A. (author)
- University of Vermont
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(creator_code:org_t)
- 2020-01-14
- 2020
- English 10 s.
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In: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 594:8, s. 1261-1270
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http://dx.doi.org/10...
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Abstract
Subject headings
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- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Immunology in the medical area (hsv//eng)
Keyword
- disulfide bond
- GxxxG
- SMIM1
- transfusion medicine
- Vel blood group system
Publication and Content Type
- art (subject category)
- ref (subject category)
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To the university's database
- By the author/editor
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Kelley, Liam P.
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Nylander, Anja
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Arnaud, Lionel
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Schmoker, Anna M ...
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St. Clair, Riley ...
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Gleason, Lindsey ...
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show more...
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Souza, Jessica M ...
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Storry, Jill R.
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Olsson, Martin L ...
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Ballif, Bryan A.
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show less...
- About the subject
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Basic Medicine
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and Immunology in th ...
- Articles in the publication
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FEBS Letters
- By the university
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Lund University