<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Pieter Rondou</style></author><author><style face="normal" font="default" size="100%">Kamila Skieterska</style></author><author><style face="normal" font="default" size="100%">Ann Packeu</style></author><author><style face="normal" font="default" size="100%">Béatrice Lintermans</style></author><author><style face="normal" font="default" size="100%">Peter Vanhoenacker</style></author><author><style face="normal" font="default" size="100%">Georges Vauquelin</style></author><author><style face="normal" font="default" size="100%">Guy Haegeman</style></author><author><style face="normal" font="default" size="100%">Kathleen Van Craenenbroeck</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">KLHL12-mediated ubiquitination of the dopamine D4 receptor does not target the receptor for degradation.</style></title><secondary-title><style face="normal" font="default" size="100%">Cell Signal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adaptor Proteins, Signal Transducing</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Arrestins</style></keyword><keyword><style  face="normal" font="default" size="100%">beta-Arrestins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Cricetinae</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoplasmic Reticulum</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Dopamine D4</style></keyword><keyword><style  face="normal" font="default" size="100%">Ubiquitination</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2010 Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">22</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;In previous studies, we identified KLHL12 as a novel interaction partner of the dopamine D4 receptor that functions as an adaptor in a Cullin3-based E3 ubiquitin ligase complex to target the receptor for ubiquitination. In this study, we show that KLHL12 promotes poly-ubiquitination of the receptor by performing ubiquitination assays in eukaryotic cells. Furthermore, we demonstrate that KLHL12 not only interacts with both immature, ER-associated and mature, plasma membrane-associated D4 receptors, but also promotes ubiquitination of both receptor subpools. Unexpectedly, however, KLHL12-mediated receptor ubiquitination does not promote proteasomal degradation of newly synthesized receptors through the ER-associated degradation pathway or lysosomal degradation of mature receptors. Moreover, our data reveal that D4 receptors do not undergo agonist-promoted ubiquitination or degradation, in contrast to many other G-protein-coupled receptors (GPCRs) indicating that ubiquitination of GPCRs does not defaultly lead to receptor degradation. Interestingly, KLHL12 does also interact with beta-arrestin2 but this has no effect on the ubiquitination or localization of beta-arrestin2 nor on the internalization of the D4 receptor.&lt;/p&gt;
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