Our last paper entitled “Substrate-induced ubiquitylation and endocytosis of yeast amino acid permeases” has been accepted for publication in the journal Molecular and Cellular Biology. This work, carried out in collaboration with Martine Prévost and Eva Krammer (ULB), reports that substrate binding to the yeast amino acid transporters Gap1 and Can1 triggers a conformational change eliciting their recognition by arrestin-like adaptors which in turn provokes their ubiquitylation by the Rsp5 ubiquitin ligase and their endocytosis. Similar mechanisms likely control many other plasma membrane secondary transporters according to the external concentration of their substrates.
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