Associated Papers
Structural basis for FLCN RagC GAP activation in MiT-TFE substrate-selective mTORC1 regulation.
Jansen RM et al.
Science Advances, 2022
Purification and biochemical characterization of the Rag GTPase heterodimer.
Doxsey DD et al.
Methods in Enzymology, 2022
Structural mechanism for amino acid-dependent Rag GTPase nucleotide state switching by SLC38A9.
Fromm SA et al.
Nature Structural & Molecular Biology, 2020
Structural mechanism of a Rag GTPase activation checkpoint by the lysosomal folliculin complex.
Lawrence RE et al.
Science (new York, N.y.), 2019
A nutrient-induced affinity switch controls mTORC1 activation by its Rag GTPase-Ragulator lysosomal scaffold.
Lawrence RE et al.
Nature Cell Biology, 2018
Hybrid Structure of the RagA/C-Ragulator mTORC1 Activation Complex.
Su MY et al.
Molecular Cell, 2017
Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1.
Zhang T et al.
Nature Communications, 2017
Intersubunit Crosstalk in the Rag GTPase Heterodimer Enables mTORC1 to Respond Rapidly to Amino Acid Availability.
Shen K et al.
Molecular Cell, 2017
Sestrins function as guanine nucleotide dissociation inhibitors for Rag GTPases to control mTORC1 signaling.
Peng M et al.
Cell, 2014
The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1.
Tsun ZY et al.
Molecular Cell, 2013
Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1.
Bar-Peled L et al.
Cell, 2012
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