<?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%">Karachaliou, Mayia</style></author><author><style face="normal" font="default" size="100%">Amillis, Sotiris</style></author><author><style face="normal" font="default" size="100%">Evangelinos, Minoas</style></author><author><style face="normal" font="default" size="100%">Kokotos, Alexandros C</style></author><author><style face="normal" font="default" size="100%">Yalelis, Vassilis</style></author><author><style face="normal" font="default" size="100%">Diallinas, George</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The arrestin-like protein ArtA is essential for ubiquitination and endocytosis of the UapA transporter in response to both broad-range and specific signals.</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Microbiol</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Arrestin</style></keyword><keyword><style  face="normal" font="default" size="100%">Aspergillus nidulans</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Mutational Analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Endocytosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Fungal Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Transport Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Metabolic Networks and Pathways</style></keyword><keyword><style  face="normal" font="default" size="100%">Proline</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Transport</style></keyword><keyword><style  face="normal" font="default" size="100%">Purines</style></keyword><keyword><style  face="normal" font="default" size="100%">Substrate Specificity</style></keyword><keyword><style  face="normal" font="default" size="100%">Ubiquitination</style></keyword><keyword><style  face="normal" font="default" size="100%">Vacuoles</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2013 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">88</style></volume><pages><style face="normal" font="default" size="100%">301-17</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">We investigated the role of all arrestin-like proteins of Aspergillus nidulans in respect to growth, morphology, sensitivity to drugs and specifically for the endocytosis and turnover of the uric acid-xanthine transporter UapA. A single arrestin-like protein, ArtA, is essential for HulA(Rsp) (5) -dependent ubiquitination and endocytosis of UapA in response to ammonium or substrates. Mutational analysis showed that residues 545-563 of the UapA C-terminal region are required for efficient UapA endocytosis, whereas the N-terminal region (residues 2-123) and both PPxY motives are essential for ArtA function. We further show that ArtA undergoes HulA-dependent ubiquitination at residue Lys-343 and that this modification is critical for UapA ubiquitination and endocytosis. Lastly, we show that ArtA is essential for vacuolar turnover of transporters specific for purines (AzgA) or l-proline (PrnB), but not for an aspartate/glutamate transporter (AgtA). Our results are discussed within the frame of recently proposed mechanisms on how arrestin-like proteins are activated and recruited for ubiquitination of transporters in response to broad range signals, but also put the basis for understanding how arrestin-like proteins, such as ArtA, regulate the turnover of a specific transporter in the presence of its substrates.</style></abstract></record></records></xml>