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J. Biol. Chem., Vol. 266, Issue 31, 20590-20593, 11, 1991
AE Mulberg, BM Tulk and M Forgac
We have previously shown that activity of a Cl- channel is required for
acidification of clathrin-coated vesicles by the coated vesicle (H+)-
ATPase (Arai, H., Pink, S. and Forgac, M. (1989) Biochemistry 28, 3075-
3082). We demonstrate that activity of the coated vesicle Cl- channel is
modulated by phosphorylation. Cl- conductance was measured in a
reconstituted preparation of coated vesicle membrane proteins using the
Cl(-)-sensitive fluorescence probe, 6-methoxy-N-(3-
sulfopropyl)quinolinium. Treatment of coated vesicle membranes with
alkaline phosphatase resulted in a 25 +/- 5% decrease in Cl- channel
activity. A parallel decrease in ATP-dependent acidification of coated
vesicles was also observed. The decrease in Cl- conductance and ATP-
dependent acidification was reversed by treatment with protein kinase A and
MgATP; the alkaline phosphatase inhibitor, sodium orthovanadate, blocked
the inhibition of acidification. These results indicate that Cl-
conductance in coated vesicles is modulated by a protein kinase A-
dependent phosphorylation and that this modulation in turn affects ATP-
dependent acidification.
Modulation of coated vesicle chloride channel activity and acidification by reversible protein kinase A-dependent phosphorylation
Department of Molecular and Cellular Physiology, Tufts University School of Medicine, Boston, Massachusetts.
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