Autor: |
Brock C; CNRS UMR5203, Montpellier F-34094 France., Boudier L, Maurel D, Blahos J, Pin JP |
Jazyk: |
angličtina |
Zdroj: |
Molecular biology of the cell [Mol Biol Cell] 2005 Dec; Vol. 16 (12), pp. 5572-8. Date of Electronic Publication: 2005 Sep 21. |
DOI: |
10.1091/mbc.e05-05-0400 |
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 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. |
Databáze: |
MEDLINE |
Externí odkaz: |
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