Journal
FEBS LETTERS
Volume 587, Issue 18, Pages 2924-2929Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2013.07.027
Keywords
mTORC1; mTOR; TIPRL; Amino acid; PP2A
Funding
- Japan Society for the Promotion of Science
- Uehara Memorial Foundation
- Grants-in-Aid for Scientific Research [24770115] Funding Source: KAKEN
Ask authors/readers for more resources
Target of rapamycin complex 1 (TORC1) has a key role in cellular regulations in response to environmental conditions. In yeast, Tip41 downregulates TORC1 signaling via activation of PP2A phosphatase. We show here that overexpression of TIPRL, a mammalian Tip41, suppressed dephosphorylation of mechanistic TORC1 (mTORC1) substrates under amino acid withdrawal, and knockdown of TIPRL conversely attenuated phosphorylation of those substrates after amino acid refeeding. TIPRL associated with the catalytic subunit of PP2A (PP2Ac), which was required for the TIPRL action on mTORC1 signaling. Collectively, unlike yeast TIP41, TIPRL has a positive effect on mTORC1 signaling through the association with PP2Ac. Structured summary of protein interactions: PP2Ac physically interacts with TIPRL by anti bait coimmunoprecipitation (View Interaction: 1, 2) PR65 physically interacts with PP2Ac by anti tag coimmunoprecipitation (View interaction) TIPRL physically interacts with PP2Ac by anti tag coimmunoprecipitation (View Interaction: 1, 2) alpha 4 physically interacts with PP2Ac by anti bait coimmunoprecipitation (View interaction) PP2Ac physically interacts with PR65 and TIPRL by anti tag coimmunoprecipitation (View interaction) PP2Ac physically interacts with TIPRL by anti tag coimmunoprecipitation (View interaction) alpha 4 physically interacts with TIPRL by anti bait coimmunoprecipitation (View Interaction: 1, 2) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available