Glycophorin A dimerization and band 3 interaction during erythroid membrane biogenesis: in vivo studies in human glycophorin A transgenic mice

Band 3 and glycophorin A (GPA) are the 2 most abundant integral proteins in the human erythrocyte membrane. Earlier studies suggested that the 2 proteins may associate not only in the mature erythrocyte membrane, but also during their posttranslational processing and intracellular trafficking. The p...

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Bibliographic Details
Published in:Blood 2001-05, Vol.97 (9), p.2872-2878
Main Authors: Auffray, Isabelle, Marfatia, Shirin, de Jong, Kitty, Lee, Gloria, Huang, Cheng-Han, Paszty, Chris, Tanner, Michael J.A., Mohandas, Narla, Chasis, Joel Anne
Format: Article
Language:English
Subjects:
Animals
Anion Exchange Protein 1, Erythrocyte - chemistry
Anion Exchange Protein 1, Erythrocyte - metabolism
BASIC BIOLOGICAL SCIENCES
Biological and medical sciences
Cell differentiation, maturation, development, hematopoiesis
Cell physiology
DIMERIZATION
Erythrocyte Membrane - chemistry
Erythrocyte Membrane - metabolism
ERYTHROCYTES
Fundamental and applied biological sciences. Psychology
Glycophorins - chemistry
Glycophorins - genetics
Glycophorins - metabolism
Humans
IN VIVO
MEMBRANES
Mice
Mice, Transgenic
Molecular and cellular biology
Protein Binding
TRANSGENIC MICE
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Summary:Band 3 and glycophorin A (GPA) are the 2 most abundant integral proteins in the human erythrocyte membrane. Earlier studies suggested that the 2 proteins may associate not only in the mature erythrocyte membrane, but also during their posttranslational processing and intracellular trafficking. The purpose of this study was to directly examine the GPA–band 3 interaction in vivo and determine the nature of this association during erythroid membrane biogenesis. Transgenic mice were generated expressing the human glycophorin A gene and were used to examine how the induction of human GPA expression affected the levels of murine GPA and band 3 expression in the red cell membrane. Murine GPA expression was reduced in erythrocytes expressing human GPA, whereas the level of band 3 expression remained constant, implying a tight coupling of band 3 and GPA expression in the membrane of mature red cells. In vivo GPA dimerization was not modulated solely by the GPA transmembrane motif, but the distance between this motif and the basic residues on the cytoplasmic side of the transmembrane domain may also be important. In addition, GPA monomers with varying degrees of glycosylation dimerized, providing clear evidence that carbohydrate structures on the extracellular domain do not affect dimerization. The association between the multiple transmembrane-spanning protein, band 3, and the single transmembrane-spanning sialoglycoprotein, GPA, may serve as a model for interactions of other multi-pass and single-pass polypeptides during membrane biogenesis.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood.V97.9.2872