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M611071200v1
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Papers In Press, published online ahead of print February 19, 2007
J. Biol. Chem, 10.1074/jbc.M611071200
Submitted on December 1, 2006
Revised on January 26, 2007
Accepted on February 19, 2007

Common structural requirements for heptahelical domain function in class A and class C GPCRS

Virginie Binet, Béatrice Duthey, Jennifer Lecaillon, Claire Vol, Julie Quoyer, Gilles Labesse, Jean-Philippe Pin, and Laurent Prézeau

Pharmacology, IGF - Institut de Genomique Fonctionnelle, Montpellier cedex 5 34094

Corresponding Author: laurent.prezeau{at}igf.cnrs.fr

G protein-coupled receptors (GPCRs) are key players in cell communication. Several classes of such receptors have been identified. Although all GPCRs possess a heptahelical domain directly activating G proteins, important structural and sequence differences within receptors from different classes suggested distinct activation mechanisms. Here we show that highly conserved charged residues likely involved in an interaction network between transmembrane domains (TM) 3 and 6 at the cytoplasmic side of class C GPCRs are critical for activation of the GABAB receptor. Indeed, the loss of function resulting from the mutation of the conserved lysine residue into aspartate or glutamate in the TM3 of GABAB2 can be partly rescued by mutating the conserved acidic residue of TM6 into either lysine or arginine. In addition, mutation of the conserved lysine into an acidic residue leads to a non-functionnal receptor that displays a high agonist affinity. This is reminiscent to a similar ionic network that constitutes a lock stabilizing the inactive state of many class A rhodopsin-like GPCRs. These data reveal that despite their original structure class C GPCRs share with class A receptors at least some common structural feature controlling G-protein activation.


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