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J. Biol. Chem., Vol. 275, Issue 24, 18219-18224, June 16, 2000
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From the The 56-kDa B1 subunit of the vacuolar
H+ATPase has a C-terminal DTAL amino acid motif
typical of PDZ-binding proteins that associate with the PDZ protein,
NHE-RF (Na+/H+ exchanger regulatory factor).
This B1 isoform is amplified in renal intercalated cells, which play a
role in distal urinary acid-base transport. In contrast, proximal
tubules express the B2 isoform that lacks the C-terminal PDZ-binding
motif. Both the B1 56-kDa subunit and the 31-kDa (E) subunit of the
H+ATPase are pulled down by glutathione S-transferase
NHE-RF bound to GSH-Sepharose beads. These subunits associate in
vivo as part of the cytoplasmic V1 portion of the
H+ATPase, and the E subunit was co-immunoprecipitated from
rat kidney cytosol with NHE-RF antibodies. The interaction of
H+ATPase subunits with NHE-RF was inhibited by a peptide
derived from the C terminus of the B1 but not the B2 isoform. NHE-RF
colocalized with H+ATPase in either the apical or the
basolateral region of B-type intercalated cells, whereas NHE-RF
staining was undetectable in A-intercalated cells. In proximal tubules,
NHE-RF was located in the apical brush border. In contrast,
H+ATPase was concentrated in a distinct membrane domain at
the base of the brush border, from which NHE-RF was absent, consistent with the expression of the truncated B2 subunit isoform in this tubule
segment. The colocalization of NHE-RF and H+ATPase in B-
but not A-intercalated cells suggests a role in generating, maintaining, or modulating the variable H+ATPase polarity
that characterizes the B-cell phenotype.
The B1 Subunit of the H+ATPase Is a PDZ
Domain-binding Protein
COLOCALIZATION WITH NHE-RF IN RENAL B-INTERCALATED CELLS*
§¶,
**,,,, and
Renal Unit and Program in Membrane Biology
and the Molecular Neurogenetics Unit, Massachusetts General
Hospital East, Charlestown, Massachusetts 02129 and the Departments
of Pathology and § Medicine,
Harvard Medical School, Boston, Massachusetts 02114
*
This work was supported by National Institutes of Health
Grants DK38452 (to S. B.), DK42956 (to D. B.), and NS24279
(to V. R.) and by a U.S. Army grant (to V. R.).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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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