Elie Saliba

TL;DR: Observations support the model that the substrate-induced conformational transition inducing endocytosis involves remodeling of cytosolic regions of the permeases, thereby promoting their recognition by arrestin-like adaptors of the Rsp5 ubiquitin ligase.

TL;DR: Transition of the plasma membrane Can1 transporter to an inward-facing conformation, as occurs during catalysis of substrate transport, provokes the unmasking of a cytosolic region targeted by the α-arrestin protein Art1, which upon activation by TORC1 recruits the Rsp5 ubiquitin ligase, thereby causing Can1 ubiquitylation and endocytosis.

TL;DR: It is found that when the endogenous Pma1 is replaced with a plant H+-ATPase, H+ influx or increase fails to activate TORC1, and that Pm1 is a key actor in this mechanism.

TL;DR: A novel pathway of Jen1p endocytosis mediated by the α-arrestin Bul1p is discovered in response to the presence of cycloheximide or rapamycin, or prolonged growth in lactate, which supports a model where conformational changes ofJen1p, associated with substrate/H+ symport, are critical for the efficiency of Bul1P-dependent Jen1P turnover.

TL;DR: It is suggested that TIPIN is important for the maintenance of DNA replication and represents a potential treatment target for the worst prognosis associated breast cancers, such as TNBC.