@article {1111,
	title = {The arrestin-like protein ArtA is essential for ubiquitination and endocytosis of the UapA transporter in response to both broad-range and specific signals.},
	journal = {Mol Microbiol},
	volume = {88},
	year = {2013},
	month = {2013 Apr},
	pages = {301-17},
	abstract = {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.},
	keywords = {Arrestin, Aspergillus nidulans, DNA Mutational Analysis, Endocytosis, Fungal Proteins, Membrane Transport Proteins, Metabolic Networks and Pathways, Proline, Protein Transport, Purines, Substrate Specificity, Ubiquitination, Vacuoles},
	issn = {1365-2958},
	doi = {10.1111/mmi.12184},
	author = {Karachaliou, Mayia and Amillis, Sotiris and Evangelinos, Minoas and Kokotos, Alexandros C and Yalelis, Vassilis and Diallinas, George}
}
