par Gournas, Christos 
;Gkionis, Stelios;Twyffels, Laure ;André, Bruno
Référence Small Meeting on Yeast Transport and Energetics (SMYTE) (34: 29/08/2016-01/09/2016: Chania, Greece)
Publication Non publié, 2016
;Gkionis, Stelios;Twyffels, Laure ;André, Bruno Référence Small Meeting on Yeast Transport and Energetics (SMYTE) (34: 29/08/2016-01/09/2016: Chania, Greece)
Publication Non publié, 2016
Poster de conférence
| Résumé : | Can1, the arginine permease of yeast, is dynamically localized in the Membrane Compartment occupied by Can1 (MCC), a plasma membrane microdomain associated with a cytoplasmic protein scaffold termed eisosome (1). Can1 undergoes ubiquitin (Ub)-dependent endocytosis in response to substrate transport (2). Yet the physiological significance of the enrichment of Can1 in the MCC with respect to its functionality and substrate-induced endocytosis remains controversial (3,4). We have now investigated the potential role of lipids and Ub in the lateral plasma membrane distribution of Can1. We found that the MCC enrichment of Can1 requires proper sphingolipid biosynthesis. In keeping with previous studies, addition of arginine promotes exit of Can1 from the MCCs. Our results show that this redistribution is dependent on Can1 activity but not on its ubiquitylation. Furthermore, an inactive Can1 mutant seems to adopt a conformation favoring its exit from the MCCs. Our data are consistent with a model where some conformational changes adopted by Can1 during substrate transport promote its segregation out of the MCCs, followed by its ubiquitylation and endocytosis. |
