{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,8]],"date-time":"2026-05-08T21:00:11Z","timestamp":1778274011231,"version":"3.51.4"},"reference-count":34,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2009,8,1]]},"abstract":"<jats:p>AE1 [anion exchanger 1, also known as SLC4A1 (solute carrier family 4, anion exchanger, member 1) and band 3 (erythrocyte membrane protein band 3)] is a major membrane glycoprotein expressed in human erythrocytes where it mediates the exchange of chloride and bicarbonate across the plasma membrane. Glycophorin A (GPA) is a sialoglycoprotein that associates with AE1 in erythrocytes forming the Wrb (Wright b) blood group antigen. These two integral proteins may also form a complex during biosynthesis, with GPA facilitating the cell surface expression of AE1. This study investigates the interaction of GPA with AE1 in K562 cells, a human erythroleukaemic cell line that expresses GPA, and the role of GPA in the cell surface expression of AE1. In K562 cells, GPA was dimeric and N- and O-glycosylated similar to erythroid GPA. GPA was localized at the cell surface, but also localized to the Golgi. AE1 expressed in K562 cells contained both complex and high-mannose oligosaccharides, and co-localized with GPA at the cell surface and in the endoplasmic reticulum (ER). The Wrb antigen was detected at the cell surface of AE1-transfected K562 cells, indicating the existence of an AE1\u2013GPA complex. Immunofluorescence and co-immunoprecipitation studies using AE1 and an ER-localized hereditary spherocytosis mutant (R760Q AE1) showed that GPA and AE1 could interact in the ER. GPA knockdown by shRNAs (small-hairpin RNAs), however, had no effect on the level of cell surface expression of AE1. The results indicate that AE1 and GPA form a complex in the ER of human K562 cells, but that both proteins can also traffic to the cell surface independently of each other.<\/jats:p>","DOI":"10.1042\/bj20090345","type":"journal-article","created":{"date-parts":[[2009,5,15]],"date-time":"2009-05-15T11:48:10Z","timestamp":1242388090000},"page":"345-356","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Interaction of anion exchanger 1 and glycophorin A in human erythroleukaemic K562 cells"],"prefix":"10.1042","volume":"421","author":[{"given":"Allison\u00a0J.","family":"Pang","sequence":"first","affiliation":[{"name":"Department of Biochemistry, University of Toronto, 1 King's College Circle, Medical Sciences Building, Toronto, Canada, M5S 1A8"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reinhart\u00a0A.\u00a0F.","family":"Reithmeier","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Toronto, 1 King's College Circle, Medical Sciences Building, Toronto, Canada, M5S 1A8"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2009,7,15]]},"reference":[{"key":"2021112215145623700_B1","first-page":"281","article-title":"Structure of the erythrocyte band 3 exchanger","volume-title":"Handbook of Biological Physics","author":"Reithmeier","year":"1996"},{"key":"2021112215145623700_B2","doi-asserted-by":"crossref","first-page":"9089","DOI":"10.1073\/pnas.86.23.9089","article-title":"Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)","volume":"86","author":"Lux","year":"1989","journal-title":"Proc. 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