RRAGC,D hydrolyzes GTP

Stable Identifier
R-HSA-9645598
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
29056322 Intersubunit Crosstalk in the Rag GTPase Heterodimer Enables mTORC1 to Respond Rapidly to Amino Acid Availability

Shen, K, Choe, A, Sabatini, DM

Mol. Cell 2017
24095279 The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1

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

Mol. Cell 2013
24081491 Recruitment of folliculin to lysosomes supports the amino acid-dependent activation of Rag GTPases

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

J. Cell Biol. 2013
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
GTPase activity of v-ATPase:Ragulator:RRAGA,B:GDP:RRAGC,D:GTP [lysosomal membrane]
Physical Entity
Activity
This event is regulated
Positively by
Orthologous Events
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Reviewed
Created