Journal article
Glycophorin A dimerization and band 3 interaction during erythroid membrane biogenesis: in vivo studies in human glycophorin A transgenic mice
Blood, Vol.97(9), pp.2872-2878
05/01/2001
DOI: 10.1182/blood.V97.9.2872
PMID: 11313283
Abstract
Abstract 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.
Details
- Title: Subtitle
- Glycophorin A dimerization and band 3 interaction during erythroid membrane biogenesis: in vivo studies in human glycophorin A transgenic mice
- Creators
- Isabelle Auffray - From the Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley; Children's Hospital Oakland Research Institute, Oakland, CA; Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY; and University of Bristol, United KingdomShirin Marfatia - From the Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley; Children's Hospital Oakland Research Institute, Oakland, CA; Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY; and University of Bristol, United KingdomKitty de Jong - From the Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley; Children's Hospital Oakland Research Institute, Oakland, CA; Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY; and University of Bristol, United KingdomGloria Lee - From the Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley; Children's Hospital Oakland Research Institute, Oakland, CA; Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY; and University of Bristol, United KingdomCheng-Han Huang - From the Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley; Children's Hospital Oakland Research Institute, Oakland, CA; Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY; and University of Bristol, United KingdomChris Paszty - From the Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley; Children's Hospital Oakland Research Institute, Oakland, CA; Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY; and University of Bristol, United KingdomMichael J. A Tanner - From the Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley; Children's Hospital Oakland Research Institute, Oakland, CA; Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY; and University of Bristol, United KingdomNarla Mohandas - From the Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley; Children's Hospital Oakland Research Institute, Oakland, CA; Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY; and University of Bristol, United KingdomJoel Anne Chasis - From the Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley; Children's Hospital Oakland Research Institute, Oakland, CA; Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY; and University of Bristol, United Kingdom
- Resource Type
- Journal article
- Publication Details
- Blood, Vol.97(9), pp.2872-2878
- DOI
- 10.1182/blood.V97.9.2872
- PMID
- 11313283
- NLM abbreviation
- Blood
- ISSN
- 0006-4971
- eISSN
- 1528-0020
- Language
- English
- Date published
- 05/01/2001
- Academic Unit
- Iowa Neuroscience Institute; Immunology; Internal Medicine
- Record Identifier
- 9984070536102771
Metrics
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