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J. Biol. Chem., Vol. 278, Issue 17, 15128-15135, April 25, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/17/15128    most recent M212315200v2 M212315200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lin, C.-Y. Articles by Barber, D. L. Search for Related Content PubMed PubMed Citation Articles by Lin, C.-Y. Articles by Barber, D. L. Social Bookmarking                      What's this?

Conserved Motifs in Somatostatin, D₂-dopamine, and _2B-Adrenergic Receptors for Inhibiting the Na-H Exchanger, NHE1^*

Chin-Yu Lin, Madhulika G. Varma, Anita Joubel, Srinivasan Madabushi^§, Olivier Lichtarge^§, and Diane L. Barber^¶

From the  University of California, San Francisco, San Francisco, California 94143 and ^§ Baylor College of Medicine, Houston, Texas 77030

Receptor subtypes within families of G protein-coupled receptors that are activated by similar ligands can regulate distinct intracellular effectors. We identified conserved motifs within intracellular domains 2 and 3 of selective subtypes of several G protein-coupled receptor families that confer coupling to the Na-H exchanger, NHE1. A T(s,p)V motif within intracellular domain 2 and a QQ(r) motif within intracellular domain 3 are shared by the somatostatin receptor subtypes SSTR1, -3, and -4, which couple to the inhibition of NHE1, but not by SSTR2 and -5, which do not signal to NHE1. Only the collective substitution of cognate SSTR2 residues with these two motifs conferred the ability of mutant SSTR2 to inhibit NHE1. Both motifs are present in D₂-dopamine receptors, which inhibit NHE1, and in _2B-adrenergic receptors, which couple to the inhibition of NHE1, but not in _2A-adrenergic receptors, which do not regulate NHE1. These findings indicate that motifs shared by different subfamilies of G protein-coupled receptors, but not necessarily by receptor subtypes within a subfamily, can confer coupling to a common effector.

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