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Regulation of transport of the angiotensin AT2 receptor by a novel membrane-associated Golgi protein.

Authors: Wruck, CJ  Funke-Kaiser, H  Pufe, T  Kusserow, H  Menk, M  Schefe, JH  Kruse, ML  Stoll, M  Unger, T 
Citation: Wruck CJ, etal., Arterioscler Thromb Vasc Biol. 2005 Jan;25(1):57-64. Epub 2004 Nov 11.
Pubmed: (View Article at PubMed) PMID:15539617
DOI: Full-text: DOI:10.1161/01.ATV.0000150662.51436.14

OBJECTIVE: Synthesis and maturation of G protein-coupled receptors are complex events that require an intricate combination of processes including protein folding, posttranslational modifications, and transport through distinct cellular compartments. Little is known concerning the regulation of G protein-coupled receptor transport from the endoplasmic reticulum to the cell surface. METHODS AND RESULTS: Here we show that the cytoplasmatic carboxy-terminal of the angiotensin AT2 receptor (AT2R) acts independently as an endoplasmic reticulum-export signal. Using a yeast two-hybrid system, we identified a Golgi membrane-associated protein termed ATBP50 (for AT2R binding protein of 50 kDa) that binds to this motif. We also cloned ATBP60 and ATBP135 encoded by the same gene as ATBP50 that mapped to chromosomes 8p21.3. Downregulation of ATBP50 using siRNA leads to retention of AT2R in inner compartments, reduced cell surface expression, and decreased antiproliferative effects of the receptor. CONCLUSIONS: Our results indicate that ATBP50 regulates the transport of the AT2R to cell membrane by binding to a specific motif within its cytoplasmic carboxy-terminal and thereby enabling the antiproliferative effects of the receptor.


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CRRD Object Information
CRRD ID: 2317014
Created: 2010-03-10
Species: All species
Last Modified: 2010-03-10
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.