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Articles in PresS, published online ahead of print November 20, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00225.2002
Submitted on May 16, 2002
Accepted on November 12, 2002
1 Medicine, UCLA, Los Angeles, CA, USA
2 Animal Cell Biochemistry, Moscow State University, Moscow, Russian Federation
* To whom correspondence should be addressed. E-mail: ikurtz{at}mednet.ucla.edu.
The electroneutral sodium bicarbonate cotransporter NBC3, co-immunoprecipitates from renal lysates with the vacuolar H+-ATPase. In renal type B intercalated cells, NBC3 co-localizes with the vacuolar H+-ATPase. The involvement of the C-termini of NBC3 and the 56 kDa subunit of the proton pump in the interaction of these proteins was investigated. The intact and modified C-termini of NBC3 and the 56 kDa subunit of the proton pump were synthesized, coupled to Sepharose beads, and used to pull-down kidney membrane proteins. Both the 56 kDa and the 70 kDa subunits of the proton pump as well as a PDZ-domain containing protein NHERF-1 were bound to the intact 18 amino acid NBC3 C-terminus. A peptide truncated by 5 C-terminal amino acids did not bind these proteins. The peptide with a C-terminal leucine changed to glycine blocked binding of both the proton pump subunits but did not affect binding of NHERF-1. The 18 amino acid C-terminus of the 56 kDa subunit of the proton pump bound NHERF-1 and NBC3 but the truncated and modified peptide did not. A complex of NBC3, the 56 kDa subunit of the proton pump, and NHERF was identified in rat kidney. The data indicate that the C-termini of NBC3 and the 56 kDa subunit of the vacuolar proton pump are PDZ-interacting motifs, which are necessary for the interaction of these proteins. NHERF-1 is involved in the interaction of NBC3 and the vacuolar proton pump.
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