A substrate localization model for the selective regulation of TORC1 downstream pathways

• Main Authors: Eigo Takeda, Akira Matsuura
• Format: Article
• Language: English
• Published: Taylor & Francis Group 2018-03-01
• Series: Communicative & Integrative Biology
• Subjects: TORC1; signal transduction; phosphoinositide; vacuoles; yeast
• Online Access: http://dx.doi.org/10.1080/19420889.2018.1475830

Target of rapamycin complex 1 (TORC1) is a protein kinase complex conserved in eukaryotes that coordinates diverse cellular processes critical for cell growth to environmental conditions. Previous studies have shown that TORC1 is localized mainly in the lysosome/vacuoles, and its localization is important for signaling to downstream pathways. We recently demonstrated that signaling to Sch9, an S6K-related substrate of TORC1 in budding yeast, was selectively suppressed upon oxidative stress, which was mediated by the delocalization of phosphatidylinositol 3, 5-bisphosphate (PI[3,5]P2) from vacuolar membranes following stress. We propose that TORC1 downstream pathways can be regulated separately via the modulation of organelle localization of a specific target protein.