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J. Biol. Chem., Vol. 275, Issue 22, 16632-16637, June 2, 2000
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From the Department of Life Science, National Creative Research
Initiative Center for Calcium and Learning, Division of Molecular and
Life Science and School of Environmental Engineering, Pohang University
of Science and Technology, Pohang 790-784, South Korea, the
§ Department of Pharmacology, Pusan National University, Kum
Jeong-ku, Pusan 609-735, South Korea, and the ¶ Department of
Medicine, Gastroenterology Division, Johns Hopkins University School of
Medicine, Baltimore, Maryland 21205
Among the phospholipase C that catalyzes the
hydrolysis of phosphatidylinositol 4,5-bisphosphate, four mammalian
phospholipase C-
Regulation of Phospholipase C-
3 Activity by
Na+/H+ Exchanger Regulatory Factor 2*
(PLC-) isotypes (isotypes 1-4) are activated
through G protein-coupled receptors (GPCRs). Although the regulation of
the PLC-s by GPCRs and heterotrimeric G proteins has been
extensively studied, little is known about the molecular determinants
that regulate their activity. The PLC- isozymes carry a putative
PSD-95/Dlg/ZO-1 (PDZ) binding motif
(X(S/T)X(V/L)COOH) at their carboxyl terminus, which is implicated in specific interactions with anchor proteins. Using the yeast two-hybrid system, we identified
Na+/H+ exchanger regulatory factor 2 (NHERF2)
as a protein that interacted with a C-terminal heptapeptide of
PLC-3. Immunoprecipitation studies revealed that NHERF2 interacts
specifically with PLC-3, but not with other PLC- isotypes.
Furthermore, PLC-3 interacted with NHERF2 rather than with other
PDZ-containing proteins. This interaction required the COOH-terminal
NTQL sequence of PLC-3 and the second PDZ domain of NHERF2.
Interestingly, NHERF2 potentiated the PLC- activation by carbachol
in COS7 and HeLa cells, while mutant NHERF2, lacking the second PDZ
domain, had no such effect. Taken together, the data suggest that
NHERF2 may act as a modulator underlying the process of
PLC-3-mediated signaling.
*
This work was supported in part by Brain Science and
Engineering Research Program Grant 98-J04-02-01-A-03, Korea Research Foundation Grant BSRI-98-4434, the National Creative Research Initiative Program of the Ministry of Science and Technology; the Korea
Science and Engineering Foundation (KOSEF) through the Center for Cell
Signaling Research at Ewha Womans University; POSTECH Research Fund
(Korea); and National Institutes of Health Grant DK-44484.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. Tel.:
82-562-279-2293; Fax: 82-562-279-2199; E-mail:
pgs@postech.ac.kr.
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