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J. Biol. Chem., Vol. 276, Issue 51, 47886-47894, December 21, 2001
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From the The cytoplasmic carboxyl-terminal domain of AE1,
the plasma membrane chloride/bicarbonate exchanger of erythrocytes,
contains a binding site for carbonic anhydrase II (CAII). To examine
the physiological role of the AE1/CAII interaction, anion exchange activity of transfected HEK293 cells was monitored by following the
changes in intracellular pH associated with AE1-mediated bicarbonate transport. AE1-mediated chloride/bicarbonate exchange was reduced 50-60% by inhibition of endogenous carbonic anhydrase with
acetazolamide, which indicates that CAII activity is required for full
anion transport activity. AE1 mutants, unable to bind CAII, had
significantly lower transport activity than wild-type AE1 (10% of
wild-type activity), suggesting that a direct interaction was required. To determine the effect of displacement of endogenous wild-type CAII
from its binding site on AE1, AE1-transfected HEK293 cells were
co-transfected with cDNA for a functionally inactive CAII mutant,
V143Y. AE1 activity was maximally inhibited 61 ± 4% in the
presence of V143Y CAII. A similar effect of V143Y CAII was found for
AE2 and AE3cardiac anion exchanger isoforms. We conclude that the
binding of CAII to the AE1 carboxyl-terminus potentiates anion
transport activity and allows for maximal transport. The interaction of
CAII with AE1 forms a transport metabolon, a membrane protein complex
involved in regulation of bicarbonate metabolism and transport.
A Transport Metabolon
FUNCTIONAL INTERACTION OF CARBONIC ANHYDRASE II AND
CHLORIDE/BICARBONATE EXCHANGERS*
§,
Membrane Transport Group and Canadian
Institutes of Health Research Group in Molecular Biology of Membrane
Proteins, Department of Physiology and Department of Biochemistry,
University of Alberta, Edmonton, Alberta T6G 2H7 and
¶ Canadian Institutes of Health Research Group in Membrane
Biology, Department of Medicine and Department of Biochemistry,
University of Toronto, Toronto, Ontario M5S 1A8, Canada
*
This research was supported by the Heart and Stroke
Foundation (to J. R. C.) and the Canadian Institutes of Health
Research (to R. A. F.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
A New Investigator of the Canadian Institutes of Health
Research and a Senior Scholar of the Alberta Heritage Foundation
for Medical Research. To whom correspondence should be addressed. Tel.:
780-492-7203; Fax: 780-492-8915; E-mail: joe.casey@ualberta.ca.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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