DIDS-effect on Ser/Thr- and Tyr-phosphorylation of membrane proteins in human erythrocytes.
Band 3, the major transmembrane multifunctional protein of human erythrocytes, has been found to be phosphorylated-dephosphorylated on both Ser/Thr- and Tyr-residues by specific protein kinases and protein phosphatases. The results reported here would indicate that the ghosts prepared from human erythrocytes pretreated with DIDS, well known inhibitor of band 3-mediated anion transport, exhibit a markedly reduced Ser/Thr-phosphorylation of spectrin and band 3, when incubated with [gamma-32P]ATP in the presence of Mg2+. On the other hand, Tyr-phosphorylation of this latter protein is practically unchanged or even slightly enhanced. This suggests that Ser/Thr- and Tyr-phosphorylation of band 3 display a different functional role.
Clari
G
G
Dipartimento di Chimica Biologica, Universita di Padova, Italy.
Bordin
L
L
Moret
V
V
D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; D012856:4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid / Q000031:analogs & derivatives* / Q000494:pharmacology; D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D001665:Binding Sites; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000097:blood / Q000737:chemistry / Q000187:drug effects*; D010766:Phosphorylation; D012694:Serine / Q000737:chemistry; D013049:Spectrin / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D013912:Threonine / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
D001457:Anion Exchange Protein 1, Erythrocyte; D008565:Membrane Proteins; D013049:Spectrin; D012856:4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; D013912:Threonine; D014443:Tyrosine; D012694:Serine; D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid