Reactome | RRAGC,D hydrolyzes GTP

RRAGC,D hydrolyzes GTP

Stable Identifier

R-HSA-9645598

Type

Reaction [transition]

Species

Homo sapiens

Compartment

lysosomal membrane

ReviewStatus

5/5

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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