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The publication of the membrane domain crystal structure made it possible to propose concrete molecular models of transport. Future research directions include improving our understanding of the transport mechanism at the molecular level and of the integrative relationships among band 3, hemoglobin, carbonic anhydrase, and gradients (both transmembrane and subcellular) of [Formula: see text], Cl<jats:sup>\u2212<\/jats:sup>, O<jats:sub>2<\/jats:sub>, CO<jats:sub>2<\/jats:sub>, pH, and nitric oxide (NO) metabolites during pulmonary and systemic capillary gas exchange. <\/jats:p>","DOI":"10.1152\/ajpcell.00275.2021","type":"journal-article","created":{"date-parts":[[2021,10,20]],"date-time":"2021-10-20T19:02:42Z","timestamp":1634756562000},"page":"C1028-C1059","update-policy":"https:\/\/doi.org\/10.1152\/aps-crossmark-policy","source":"Crossref","is-referenced-by-count":74,"title":["Cell physiology and molecular mechanism of anion transport by erythrocyte band 3\/AE1"],"prefix":"10.1152","volume":"321","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5235-4597","authenticated-orcid":true,"given":"Michael 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