Inhibition of TORC1 signaling induces a variety of cellular changes indicative of a starvation response, including a reduction in protein synthesis, enlargement of the vacuole, activation and repression of gene transcription, and induction of autophagy (Zoncu et al. 2011). Amino acid biosynthesis and sorting of amino acid permeases are also impacted when TORC1 is inhibited in response to starvation. For example, various high affinity amino acid permeases are relocalized in the cell, changing the import of certain classes of amino acids. Well-established examples of this are the effects on the high-affinity tryptophan permease, Tat2, and the general amino acid permease, Gap1 (Beck et al. 1999). In rich media, Tat2 is stable and imports tryptophan. Upon the inhibition of TORC1 signaling that results from nitrogen deprivation, the phosphatase Tap42 dephosphorylates Npr1, a serine/threonine kinase, rendering Npr1 active. Activated Npr1 then mediates the degradation of Tat2 and localization of Gap1 to the plasma membrane (Schmidt et al. 1998; Beck et al. 1999). Consequently, Gap1 becomes responsible for the import of amino acids, including tryptophan. Notably, several members of the SEA complex have genetic interactions with factors that regulate Gap1 localization, such as Lst8, a component of the TOR signaling pathway, and share fitness profiles across numerous chemical and environmental stress conditions with genes involved in Gap1 sorting (Dokudovskaya et al. 2011; Hillenmeyer et al. 2008).