Fig. 6: Model of signaling through the SEAC.
From: Structure and function of the yeast amino acid-sensing SEAC–EGOC supercomplex
a, Immunoblots of phosphorylated and total Sch9 after starvation and repletion of amino acids (AA) in WT, SEACCDΔsea2, SEACCD and Δsea2 cells. b, Quantification of relative Sch9 phosphorylation over 30 min of starvation and amino acid repletion in WT, SEACCDΔsea2 and SEACCD cells. Data from three independent experiments are presented as mean values ± s.d. c, Quantification of relative Sch9 phosphorylation over 30 min of starvation and amino acid repletion in WT, SEACCDΔsea2 and Δsea2 cells. Data from three independent experiments are presented as mean values ± s.d. d, A model of regulation of the SEAC on the vacuolar membrane. We propose that the GAP activity regulates the GTP loading of the EGOC, which self-limits localization of the SEAC to the vacuole membrane. The interplay between the N-terminal propeller of Sea2 and the catalytic arginine finger of Npr2 remains unclear and, if it exists, would probably require the function of an as of yet unknown factor.
