RRAGC,D hydrolyzes GTP

Stable Identifier
Reaction [transition]
Homo sapiens
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RRAGC (RagC) and RRAGD (RagD) are guanyl nucleotide-binding proteins that hydrolyze GTP (Tsun et al. 2013, Shen et al. 2017). The GDP-bound form of RRAGC,D is the active form that recruits mTORC1 to the lysosomal membrane (Tsun et al. 2013). RRAGC,D forms a heterodimer with RRAGA,B that has two stable conformations: RRAGA,B:GTP:RRAGC,D:GDP (active) or RRAGA,B:GDP:RRAGC,D:GTP (inactive) (Shen et al. 2017). Folliculin (FLCN) complexed with FNIP1 or FNIP2 interacts with RRAGA (Petit et al. 2013) and acts as a GTPase activator (GAP) for RRAGC:GTP and RRAGD:GTP (Tsun et al. 2013). FLCN is located at the lysosomal membrane during amino acid starvation and in the cytosol during amino acid stimulation (Tsun et al. 2013).
Literature References
PubMed ID Title Journal Year
24095279 The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1

Sabatini, DM, Wang, T, Zoncu, R, Spooner, E, Tsun, ZY, Bar-Peled, L, Chantranupong, L, Kim, C

Mol. Cell 2013
29056322 Intersubunit Crosstalk in the Rag GTPase Heterodimer Enables mTORC1 to Respond Rapidly to Amino Acid Availability

Sabatini, DM, Choe, A, Shen, K

Mol. Cell 2017
24081491 Recruitment of folliculin to lysosomes supports the amino acid-dependent activation of Rag GTPases

Ferguson, SM, Petit, CS, Roczniak-Ferguson, A

J. Cell Biol. 2013
Catalyst Activity

GTPase activity of v-ATPase:Ragulator:RRAGA,B:GDP:RRAGC,D:GTP [lysosomal membrane]

This event is regulated
Positively by
Orthologous Events
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