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J Biol Chem, Vol. 274, Issue 42, 29843-29849, October 15, 1999
From the The epithelial isoform of the
Na+/H+ exchanger, NHE3, associates with
at least two related regulatory factors called NHERF1/EBP50 and
NHERF2/TKA-1/E3KARP. These factors in addition interact with the
cytoskeletal protein ezrin, which in turn binds to actin. The possible
linkage of NHE3 with the cytoskeleton prompted us to test the effect of
actin-modifying agents on NHE3 activity. Cytochalasins B and D and
latrunculin B, which interfere with actin polymerization, induced a
profound inhibition of NHE3 activity. The effect was isoform-specific
inasmuch as the "housekeeping" exchanger NHE1 was virtually
unaffected. Cytoskeletal disorganization was associated with a
subcellular redistribution of NHE3, which accumulated at sites where
actin aggregated, suggesting a physical interaction of exchangers with
the cytoskeleton. An interaction was further suggested by the
co-sedimentation of a detergent-insoluble fraction of NHE3 with the
actin cytoskeleton. Inhibition of transport was not due to diminution
in the number of transporters at the plasmalemma. Functional analyses
of NHE1/NHE3 chimeras revealed that the cytoplasmic domain of NHE3
conferred sensitivity to cytochalasin B. Progressive carboxyl-terminal
and internal deletions of the cytoplasmic region of NHE3 indicated that
the region between residues 650 and 684 is critical for this response.
This region overlaps with the domain reported to interact with NHERF
and also contains a putative ezrin-binding site; hence, it likely plays
a role in interactions with the cytoskeleton.
The Apical Na+/H+ Exchanger Isoform NHE3
Is Regulated by the Actin Cytoskeleton
,,,,
, and
Cell Biology Programme, The Hospital for
Sick Children Research Institute, Toronto, Ontario M5G 1X8 and
Department of Physiology, McGill University,
Montreal, Quebec H3G 1Y6, Canada
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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