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J. Biol. Chem., Vol. 277, Issue 28, 25239-25246, July 12, 2002
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From the Canadian Institutes of Health Research Membrane
Protein Research Group, Departments of Physiology and Biochemistry,
University of Alberta, Edmonton, Alberta T6G 2H7, Canada
Cytosolic carbonic anhydrase II (CAII) and the
cytoplasmic C-terminal tails of chloride/bicarbonate anion exchange
(AE) proteins associate to form a bicarbonate transport metabolon,
which maximizes the bicarbonate transport rate. To determine whether
cell surface-anchored carbonic anhydrase IV (CAIV) interacts with AE
proteins to accelerate the bicarbonate transport rate, AE1-mediated
bicarbonate transport was monitored in transfected HEK293 cells.
Expression of the inactive CAII V143Y mutant blocked the interaction
between endogenous cytosolic CAII and AE1, AE2, and AE3 and inhibited
their transport activity (53 ± 3, 49 ± 10, and 35 ± 1% inhibition, respectively). However, in the presence of V143Y CAII,
expression of CAIV restored full functional activity to AE1, AE2, and
AE3 (AE1, 101 ± 3; AE2, 85 ± 5; AE3, 108 ± 1%). In
Triton X-100 extracts of transfected HEK293 cells, resolved by sucrose
gradient ultracentrifugation, CAIV recruitment to the position of AE1
suggested a physical interaction between CAIV and AE1. Gel overlay
assays showed a specific interaction between CAIV and AE1, AE2, and
AE3. Glutathione S-transferase pull-down assays
revealed that the interaction between CAIV and AE1 occurs on the large
fourth extracellular loop of AE1. We conclude that AE1 and CAIV
interact on extracellular loop 4 of AE1, forming the extracellular
component of a bicarbonate transport metabolon, which accelerates the
rate of AE-mediated bicarbonate transport.
The Extracellular Component of a Transport Metabolon
EXTRACELLULAR LOOP 4 OF THE HUMAN AE1
Cl
/HCO
,
*
This work was supported in part by the Heart and Stroke
Foundation of Canada. A preliminary version of this work was published previously in abstract form (1).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.
Supported by studentship trainee awards from the Heart and Stroke
Foundation of Canada and the Alberta Heritage Foundation for Medical Research.
§
Supported by a postdoctoral fellowship from the Alberta Heritage
Foundation for Medical Research.
¶
Senior Scholar of the Alberta Heritage Foundation for Medical
Research. To whom correspondence should be addressed. Dept. of
Physiology, University of Alberta Edmonton, Alberta T6G 2H7, Canada.
Tel.: 780-492-7203; Fax: 780-492-8915; E-mail:
joe.casey@ualberta.ca.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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