@article{3086304,
    title = "The α-Arrestin Bul1p Mediates Lactate Transporter Endocytosis in Response to Alkalinization and Distinct Physiological Signals",
    author = "Talaia, G. and Gournas, C. and Saliba, E. and Barata-Antunes, C. and Casal, M. and André, B. and Diallinas, G. and Paiva, S.",
    journal = "JOURNAL OF MOLECULAR BIOLOGY",
    year = "2017",
    volume = "429",
    number = "23",
    pages = "3678-3695",
    publisher = "INSTAP Academic Press",
    issn = "0022-2836",
    doi = "10.1016/j.jmb.2017.09.014",
    keywords = "alpha arrestin Bul1p;  cycloheximide;  hydrogen;  lactic acid;  rapamycin;  retina S antigen;  unclassified drug;  alkali;  BUL1 protein, S cerevisiae;  cotransporter;  JEN1 protein, S cerevisiae;  monocarboxylate transporter;  NPR1 protein, S cerevisiae;  phosphoprotein phosphatase 2;  protein kinase;  retina S antigen;  Saccharomyces cerevisiae protein;  SIT4 protein, S cerevisiae;  ubiquitin protein ligase, alkalinization;  Article;  controlled study;  endocytosis;  fungal cell;  fungal strain;  fungus growth;  nonhuman;  pH;  pleiotropy;  priority journal;  protein conformation;  protein degradation;  protein expression;  protein localization;  protein metabolism;  protein processing;  Saccharomyces cerevisiae;  signal transduction;  ubiquitination;  cell membrane;  drug effects;  endocytosis;  growth, development and aging;  metabolism;  physiology;  transport at the cellular level, Alkalies;  Arrestin;  Biological Transport;  Cell Membrane;  Endocytosis;  Metabolic Networks and Pathways;  Monocarboxylic Acid Transporters;  Protein Kinases;  Protein Phosphatase 2;  Saccharomyces cerevisiae;  Saccharomyces cerevisiae Proteins;  Signal Transduction;  Symporters;  Ubiquitin-Protein Ligases",
    abstract = "Eukaryotic α-arrestins connect environmental or stress signaling pathways to the endocytosis of plasma membrane transporters or receptors. The Saccharomyces cerevisiae lactate transporter Jen1p has been used as a model cargo for elucidating the mechanisms underlying endocytic turnover in response to carbon sources. Here, we discover a novel pathway of Jen1p endocytosis mediated by the α-arrestin Bul1p in response to the presence of cycloheximide or rapamycin, or prolonged growth in lactate. While cycloheximide or rapamycin modify cells pleiotropically, the major effect of prolonged growth in lactate was shown to be external pH alkalinization. Importantly, employment of specific inactive Jen1p versions showed that Bul1p-dependent endocytosis requires lactate transport, according to the signal imposed. Our results support a model where conformational changes of Jen1p, associated with substrate/H+ symport, are critical for the efficiency of Bul1p-dependent Jen1p turnover. © 2017 Elsevier Ltd"
}