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MBC in Press, published online ahead of print September 21, 2005
Mol. Biol. Cell 10.1091/mbc.E05-05-0400

A more recent version of this article appeared on December 1, 2005
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Submitted on May 6, 2005
Revised on September 8, 2005
Accepted on September 12, 2005

Assembly-dependent Surface Targeting of the Heterodimeric GABAB Receptor Is Controlled by COPI, But Not 14-3-3

Carsten Brock, Laure Boudier, Damien Maurel, Jaroslav Blahos,* and Jean-Philippe Pin

CNRS UMR5203, INSERM U661, University of Montpellier I, University of Montpellier II, and Département de Pharmacologie Moléculaire, Institut de Génomique Fonctionnelle, Montpellier F-34094 Cedex 5, France

Monitoring Editor: Akihiko Nakano

Cell surface expression of transmembrane proteins is strictly regulated. Mutually exclusive interaction with COPI or 14-3-3 proteins has been proposed as a mechanism underlying such trafficking control of various proteins. In particular, 14-3-3 dimers have been proposed to "sense" correctly assembled oligomers, allowing their surface targeting by preventing COPI-mediated intracellular retention. Here we examined whether such a mechanism is involved in the quality control of the heterodimeric G protein-coupled GABAB receptor. Its GB1 subunit, carrying the retention signal RSR, only reaches the cell surface when associated with the GB2 subunit. We show that COPI and 14-3-3 specifically bind to the GB1 RSR sequence, and that COPI is involved in its intracellular retention. However, we demonstrate that the interaction with 14-3-3 is not required for proper function of the GABAB receptor quality control. Accordingly, competition between 14-3-3 and COPI cannot be considered as a general trafficking control mechanism. A possible other role for competition between COPI and 14-3-3 binding is discussed.

*Present address: Department of Molecular Pharmacology, Institute of Experimental Medicine, Academie of Science of the Czech Republic, Videnska 1083, 142 20 Prague 4, Czech Republic.

Address correspondence to: Jean-Philippe Pin (jppin{at}igf.cnrs.fr)




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