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1 Division of Nephrology, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA
2 Department of Physics, Case Western Reserve University, Cleveland, OH 44106, USA
We have recently shown that carbonic anhydrase II (CAII) binds in vitro to the C-terminus of the electrogenic sodium bicarbonate cotransporter kNBC1 (kNBC1-ct). In the present study we determined the molecular mechanisms for the interaction between the two proteins and whether kNBC1 and CAII form a transport metabolon in vivo wherein bicarbonate is transferred from CAII directly to the cotransporter. Various residues in the C-terminus of kNBC1 were mutated and the effect of these mutations on both the magnitude of CAII binding and the function of kNBC1 expressed in mPCT cells was determined. Two clusters of acidic amino acids, L958DDV and D986NDD in the wild-type kNBC1-ct involved in CAII binding were identified. In both acidic clusters, the first aspartate residue played a more important role in CAII binding than others. A significant correlation between the magnitude of CAII binding and kNBC1-mediated flux was shown. The results indicated that CAII activity enhances flux through the cotransporter when the enzyme is bound to kNBC1. These data are the first direct evidence that a complex of an electrogenic sodium bicarbonate cotransporter with CAII functions as a transport metabolon.
(Received 22 March 2004;
accepted after revision 23 June 2004;
first published online 24 June 2004)
Corresponding authors I. Kurtz and A. Pushkin: UCLA Division of Nephrology, 10833 Le Conte Avenue, Room 7-155 Factor Building, Los Angeles, CA 90095-1689, USA. Email: ikurtz{at}mednet.ucla.edu and apushkin{at}mednet.ucla.edu
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