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J. Biol. Chem., Vol. 277, Issue 26, 23714-23724, June 28, 2002
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From the Two PDZ domain-containing proteins, NHERF
and E3KARP are necessary for cAMP-dependent inhibition of
Na+/H+ exchanger 3 (NHE3). In this study,
we demonstrate a specific role of E3KARP, which is not duplicated by
NHERF, in Ca2+-dependent inhibition of NHE3
activity. NHE3 activity is inhibited by elevation of intracellular
Ca2+ ([Ca2+]i) in PS120 fibroblasts
stably expressing E3KARP but not those expressing NHERF. In addition,
this Ca2+-dependent inhibition requires
Ca2+-dependent association between
Ca2+-dependent Inhibition of
Na+/H+ Exchanger 3 (NHE3) Requires an
NHE3-E3KARP-
-Actinin-4 Complex for Oligomerization and
Endocytosis*
,,, and¶
Departments of Medicine and
¶ Physiology, Gastrointestinal Division, The Johns Hopkins
University School of Medicine, Baltimore, Maryland 21205 and the
§ Division of Molecular and Life Science, Pohang University
of Science and Technology, San 31, Pohang 790-784, Republic of Korea
-actinin-4 and E3KARP. NHE3 is indirectly connected to -actinin-4
in a protein complex through Ca2+-dependent
interaction between -actinin-4 and E3KARP, which occurs through the
actin-binding domain plus spectrin repeat domain of -actinin-4.
Elevation of [Ca2+]i results in oligomerization
and endocytosis of NHE3 as well as in inhibition of NHE3 activity.
Overexpression of -actinin-4 potentiates the inhibitory effect of
ionomycin on NHE3 activity by accelerating the oligomerization and
endocytosis of NHE3. In contrast, overexpression of the actin-binding
domain plus spectrin repeat domain acts as a dominant-negative mutant
and prevents the inhibitory effect of ionomycin on NHE3 activity as
well as the oligomerization and internalization of NHE3. From these
results, we propose that elevated Ca2+ inhibits NHE3
activity through oligomerization and endocytosis of NHE3, which
occurs via formation of an NHE3-E3KARP--actinin-4 complex.
*
This work was supported in part by National Institutes of
Health Grant RO1 DK26523, PO1 DK44484, and The Hopkins Center for Epithelial Disorders.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.
To whom correspondence should be addressed: GI Division, Dept.
of Medicine, The Johns Hopkins University School of Medicine, 925 Ross
Research Bldg., 720 Rutland Ave., Baltimore, MD 21205. Tel.:
410-955-9685; Fax: 410-955-9677; E-mail: mdonowit@jhmi.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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