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J. Biol. Chem., Vol. 277, Issue 36, 32954-32962, September 6, 2002
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From the Regulators of G protein signaling (RGS)
constitute a family of proteins with a conserved RGS domain of ~120
amino acids that accelerate the intrinsic GTP hydrolysis of activated
G
Interaction of 14-3-3 Protein with Regulator of G
Protein Signaling 7 Is Dynamically Regulated by Tumor Necrosis
Factor-
*
§,§,,,
, and
Renal Division and Center for Clinical
Research, University Hospital Freiburg, Hugstetterstrasse 55, 79106 Freiburg, Germany and the ¶ German Cancer Research Center, Im
Neuenheimer Feld 280, 69120 Heidelberg, Germany
i and Gq subunits. The
phosphorylation-dependent interaction of 14-3-3 proteins
with a subset of RGS proteins inhibits their GTPase-accelerating activity in vitro. The inhibitory interaction between
14-3-3 and RGS7 requires phosphorylation of serine 434 of RGS7. We now
show that phosphorylation of serine 434 is dynamically regulated by TNF-. Cellular stimulation by TNF- transiently decreased the phosphorylation of serine 434 of RGS7, abrogating the inhibitory interaction with 14-3-3. We examined the effect of 14-3-3 on
RGS-mediated deactivation kinetics of G protein-coupled inwardly
rectifying K+ channels (GIRKs) in Xenopus
oocytes. 14-3-3 inhibited the function of wild-type RGS7, but not that
of either RSG7P436R or RGS4, two proteins that do not bind
14-3-3. Our findings are the first evidence that extracellular signals
can modulate the activity of RGS proteins by regulating their
interaction with 14-3-3.
*
This work was supported by grants of the Deutsche
Forschungsgemeinschaft (to T. B., G. W., and E. K.).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 and reprint requests should be
addressed: Renal Division, University Hospital Freiburg,
Hugstetterstrasse 55, 79106 Freiburg, Germany. Tel.: 49-761-270-3251;
Fax: 49-761-270-3245; E-mail:
walz@med1.ukl.uni-freiburg.de.
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