Function and regulation of amino acid transporters : insights from predicted structure

In collaboration with Dr. Martine Prévost and Dr. Eva-Maria Kramer (Structure and Function of Biological Membranes, ULB), we used the recently solved crystal structure of a bacterial amino acid transporter as a template to build 3D atomic models of several yeast amino acid transporters (Gournas et al. 2016). This allowed us to study how these proteins recognize their amino acid substrates, and using this knowledge we could convert the arginine-specific permease into a lysine-specific permease (Ghaddar et al. 2014a). We also obtained evidence that a substrate-elicited change of conformation of the Gap1 permease promotes its recognition by the Bul arrestins thereby trigger its ubiquitylation (Ghaddar et al. 2014b).