Affordable Access

deepdyve-link
Publisher Website

The Rag GTPase-Ragulator complex attenuates TOR complex 1 signaling in fission yeast.

Authors
  • Fukuda, Tomoyuki1, 2
  • Shiozaki, Kazuhiro1, 3
  • 1 a Graduate School of Biological Sciences , Nara Institute of Science and Technology , Ikoma , Nara , Japan. , (Japan)
  • 2 b Department of Cellular Physiology , Niigata University Graduate School of Medical and Dental Sciences , Niigata , Japan. , (Japan)
  • 3 c Department of Microbiology and Molecular Genetics , University of California , Davis , CA USA.
Type
Published Article
Journal
Autophagy
Publisher
Landes Bioscience
Publication Date
Jan 01, 2018
Volume
14
Issue
6
Pages
1105–1106
Identifiers
DOI: 10.1080/15548627.2018.1444313
PMID: 29799770
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Target of rapamycin complex 1 (TORC1) is an evolutionarily conserved protein kinase complex, whose activation in response to nutrients suppresses autophagy. In mammalian cells, amino-acid stimuli induce lysosomal translocation and activation of MTORC1 through the RRAG GTPase heterodimer, which is tethered to the surface of lysosomes by the Ragulator complex. Our recent study demonstrated that the fission yeast Schizosaccharomyces pombe also has a Ragulator complex that anchors the Gtr1-Gtr2 Rag GTPase heterodimer to the vacuole, a lysosome-like organelle. Unexpectedly, however, neither vacuolar localization nor activation of TORC1 is dependent on the Rag-Ragulator complex, which instead plays a critical role in attenuating TORC1 signaling. Our findings suggest dual functionality of the Rag GTPase in both activation and inactivation of TORC1.

Report this publication

Statistics

Seen <100 times