Functional correlation between the Ser/Thr-phosphorylation of band-3 and band-3-mediated transmembrane anion transport in human erythrocytes.
In human erythrocytes, okadaic acid, a potent inhibitor of certain protein phosphatases, promotes a marked increase of Ser/Thr-phosphorylation of membrane proteins, including band-3 protein. Moreover, okadaic acid also increases the band-3-mediated oxalate transport across the membranes, thus suggesting that this process is regulated by Ser/Thr-phosphorylation of transporter band-3 protein.
Istituto di Medicina Interna, Università di Padova, Italy.
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D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism* / Q000502:physiology*; D001692:Biological Transport / Q000187:drug effects; D004912:Erythrocytes / Q000187:drug effects*; D004988:Ethers, Cyclic / Q000494:pharmacology; D006801:Humans; D019319:Okadaic Acid; D010070:Oxalates / Q000493:pharmacokinetics; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors; D010766:Phosphorylation; D012694:Serine / Q000378:metabolism*; D013912:Threonine / Q000378:metabolism*
D001457:Anion Exchange Protein 1, Erythrocyte; D004988:Ethers, Cyclic; D010070:Oxalates; D019319:Okadaic Acid; D013912:Threonine; D012694:Serine; D010749:Phosphoprotein Phosphatases