The hydrophobic amino acid residues in the membrane-proximal C tail of the G protein-coupled vasopressin V2 receptor are necessary for transport-competent receptor folding

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Item Type:	Article
Title:	The hydrophobic amino acid residues in the membrane-proximal C tail of the G protein-coupled vasopressin V2 receptor are necessary for transport-competent receptor folding
Creators Name:	Thielen, A., Oueslati, M., Hermosilla, R., Krause, G., Oksche, A., Rosenthal, W. and Schuelein, R.
Abstract:	It is believed that the membrane-proximal C tail of the G protein-coupled receptors forms an additional alpha helix with amphipathic properties (helix 8). It was previously shown for the vasopressin V2 receptor (V2R) that a conserved dileucine motif (L(339), L(340)) in this putative helix 8 is necessary for endoplasmic reticulum (ER) to Golgi transfer of the receptor. Here, we demonstrate that the other hydrophobic residues forming the non-polar side of this helix (F(328), V(332) and L(336)) are also transport-relevant. In contrast, the multiple serine residues contributing to the more hydrophilic side (S(330), S(331), S(333), S(334), S(338)) do not influence receptor trafficking. In addition, we show unambiguously by the use of pharmacological chaperones that the hydrophobic residues of the putative helix 8 do not form a transport signal necessary for receptor sorting into ER to Golgi vesicles. Instead, they are necessary to establish a transport-competent folding state in the early secretory pathway.
Keywords:	Vasopressin V2 Receptor, G Protein-Coupled Receptor, Receptor Trafficking, C Tail, Endoplasmic Reticulum, Quality Control System, Transport Motif, Animals
Source:	FEBS Letters
ISSN:	0014-5793
Publisher:	Elsevier
Volume:	579
Number:	23
Page Range:	5227-5235
Date:	26 September 2005
Official Publication:	https://doi.org/10.1016/j.febslet.2005.08.043
PubMed:	View item in PubMed

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