Cytosolic protein binding to band-3 protein inhibits endocytosis of isolated human erythrocyte membranes.
Recent studies of haemoglobin binding to the cytoplasmic side of the erythrocyte membrane have shown that the predominant high-affinity interaction occurs with the major integral membrane protein known as band-3 protein and that this interaction may occur within the intact erythrocyte in a manner regulated by cell pH. We report here that haemoglobin and glyceraldehyde 3-phosphate dehydrogenase binding to band-3 protein in isolated membranes can inhibit endocytosis during vesiculation in vitro. The specificity of this effect was demonstrated by showing that myoglobin, which has an affinity for the membrane fully one to two orders of magnitude lower than that for haemoglobin, does not inhibit endocytosis.
D001457:Anion Exchange Protein 1, Erythrocyte; D001798:Blood Proteins / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D004705:Endocytosis / Q000187:drug effects*; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism / Q000502:physiology*; D004912:Erythrocytes / Q000502:physiology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000494:pharmacology*; D006441:Hemoglobin A / Q000494:pharmacology*; D006801:Humans; D066298:In Vitro Techniques; D009211:Myoglobin / Q000494:pharmacology; D011485:Protein Binding
D001457:Anion Exchange Protein 1, Erythrocyte; D001798:Blood Proteins; D009211:Myoglobin; D006441:Hemoglobin A; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases