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  • Title: Tyrosine-protein kinase inhibition in human erythrocytes by polyphosphoinositides (PIP and PIP2).
    Author: Bordin L, Clari G, Baggio B, Moret V.
    Journal: Biochem Biophys Res Commun; 1992 Sep 16; 187(2):853-8. PubMed ID: 1382423.
    Abstract:
    In human erythrocytes Ser/Thr- and Tyr-phosphorylations of cytoplasmic domain of band 3 are catalyzed by casein kinase I and Tyr-protein kinase respectively, both distributed between cytosol and membrane structures. The results reported here show that purified cytosolic Tyr-protein kinase activity, assayed on added substrates such as poly(Glu,Tyr)4:1 and isolated chymotryptic fragments of band 3 cytoplasmic domain (cdb3), is potently inhibited by PIP and even more by PIP2. Similar inhibitory effects are displayed by these polyphosphoinositides also on the endogenous Tyr-phosphorylation of band 3, when they are added to the isolated native membranes, thus suggesting their involvement in regulating in-vivo Tyr-phosphorylation of membrane proteins.
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