Amino Acids Stimulate TORC1 through Lst4-Lst7, a GTPase-Activating Protein Complex for the Rag Family GTPase Gtr2
- Péli-Gulli, Marie-Pierre Department of Biology, University of Fribourg, Switzerland -
- Sardu, Alessandro Department of Biology, University of Fribourg, Switzerland -
- Panchaud, Nicolas Department of Biology, University of Fribourg, Switzerland -
- Raucci, Serena Department of Biology, University of Fribourg, Switzerland
- De Virgilio, Claudio Department of Biology, University of Fribourg, Switzerland
-
06.10.2015
Published in:
- Cell Reports. - 2015, vol. 13, no. 1, p. 1–7
English
Rag GTPases assemble into heterodimeric complexes consisting of RagA or RagB and RagC or RagD in higher eukaryotes, or Gtr1 and Gtr2 in yeast, to relay amino acid signals toward the growth-regulating target of rapamycin complex 1 (TORC1). The TORC1-stimulating state of Rag GTPase heterodimers, containing GTP- and GDP-loaded RagA/B/Gtr1 and RagC/D/Gtr2, respectively, is maintained in part by the FNIP-Folliculin RagC/D GAP complex in mammalian cells. Here, we report the existence of a similar Lst4-Lst7 complex in yeast that functions as a GAP for Gtr2 and that clusters at the vacuolar membrane in amino acid-starved cells. Refeeding of amino acids, such as glutamine, stimulated the Lst4-Lst7 complex to transiently bind and act on Gtr2, thereby entailing TORC1 activation and Lst4-Lst7 dispersal from the vacuolar membrane. Given the remarkable functional conservation of the RagC/D/Gtr2 GAP complexes, our findings could be relevant for understanding the glutamine addiction of mTORC1-dependent cancers.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
-
- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 257843
- DOI 10.1016/j.celrep.2015.08.059
- Persistent URL
- https://folia.unifr.ch/unifr/documents/304622
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