Abstract
Mutations of the anion exchanger 1 (AE1, SLC4A1, also called band 3) cause erythroid disorders of hereditary spherocytosis, hereditary stomatocytosis, and ovalocytosis associated with hemolytic anemia. A largely discrete set of AE1 mutations causes familial distal renal tubular acidosis. Red cell phenotypes are attributed to the disordered membrane stability or the cation leak, while most cases of the distal renal tubular acidosis are caused by abnormal AE1 trafficking. A growing body of structure-function data obtained from pathobiology of AE1 mutants, together with emerging information about physiological structure and function, is advancing our understanding of this multifunctional polytopic membrane protein, AE1.
