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J. Biol. Chem., Vol. 275, Issue 32, 24590-24594, August 11, 2000
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From the Department of Cell Biology and Physiology,
University of New Mexico Health Science Center, Albuquerque, New
Mexico 87131
Following activation by ligand, the
N-formyl peptide receptor (FPR) undergoes processing events
initiated by phosphorylation that lead to receptor desensitization and
internalization. Our previous results have shown that FPR
internalization can occur in the absence of receptor desensitization,
suggesting that FPR desensitization and internalization are controlled
by distinct mechanisms. More recently, we have provided evidence that
internalization of the FPR occurs via a mechanism that is independent
of the actions of arrestin, dynamin, and clathrin. In the present
report, we demonstrate that stimulation of the FPR with agonist leads
to a significant translocation of arrestin-2 from the cytosol to the
membrane. Fluorescence microscopy revealed that the translocated arrestin-2 is highly colocalized with the ligand-bound FPR. A D71A
mutant FPR, which does not undergo activation or phosphorylation in
response to ligand, did not colocalize with arrestin-2. Surprisingly, an R123G mutant FPR, which does not bind G protein but does become phosphorylated and subsequently internalized, also did not bind arrestin. These results indicate that arrestin binding is not required
for FPR internalization and demonstrate for the first time that a
common motif, the conserved "DRY" domain of G protein-coupled receptors, is essential for phosphorylation-dependent arrestin binding, as well as G protein activation.
Arrestin Binding to the G Protein-coupled N-Formyl
Peptide Receptor Is Regulated by the Conserved "DRY" Sequence*
*
This research was supported by Grants AI36357 and AI43932
from the National Institutes of Health and a grant-in-aid from the American Heart Association (National Center), and the University of New
Mexico Cancer Center was supported by the New Mexico State Cigarette
Tax.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.
Tel.: 505-272-5647; Fax: 505-272-1448; E-mail:
eprossnitz@salud.unm. edu.
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