A Comprehensive Membrane Interactome Mapping of Sho1p Reveals Fps1p as a Novel Key Player in the Regulation of the HOG Pathway in S. cerevisiae.

摘要: Sho1p, an integral membrane protein, plays a vital role in the high-osmolarity glycerol (HOG) mitogen-activated protein kinase pathway yeast Saccharomyces cerevisiae. Activated under conditions of high osmotic stress, it interacts with other HOG proteins to mediate cell signaling events, ensuring that cells can adapt and remain viable. In attempt further understand how function Sho1p is regulated through its protein–protein interactions (PPIs), we identified 49 unique PPIs use two-hybrid (MYTH), assay specifically suited identify full-length their native environment. Secondary validation by literature search, or two complementary PPI assays, confirmed 80% these interactions, resulting high-quality interactome. This set putative included both previously characterized interactors, along large subset interactors have not been as binding Sho1p. The SH3 domain was found be important for many interactors. One particular novel interactor interest transporter Fps1p, which shown require via N-terminal soluble regulatory domain. Furthermore, Fps1p involved positive regulation phosphorylation downstream Hog1p. study represents largest interactome analysis date complements past studies on increasing our understanding regulation.