Assembly-dependent Surface Targeting of the Heterodimeric GABABReceptor Is Controlled by COPI but Not 14-3-3

Autor: Brock, Carsten, Boudier, Laure, Maurel, Damien, Blahos, Jaroslav, Pin, Jean-Philippe
Zdroj: Molecular Biology of the Cell; December 2005, Vol. 16 Issue: 12 p5572-5578, 7p
Abstrakt: 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 GABABreceptor. 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 GABABreceptor 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.
Databáze: Supplemental Index