The minimal, reusable nucleotide-switch motif shared by regulatory GTPases: a guanine-nucleotide exchange factor (GEF) loads GTP to flip the GTPase into its active conformation, where it engages downstream effectors; a GTPase-activating protein (GAP) then stimulates GTP hydrolysis to return the switch to its inactive GDP-bound state. The motif is deliberately gene-free and taxon-neutral: it fixes only the GEF/GTPase/GAP roles (by molecular-function term) and the load/hydrolyze topology. Concrete switches - the Ras, Rho/Rac/Cdc42, Rab, Arf, Ran, and heterotrimeric-Galpha families - embed this motif as an inner bundle through `conforms_to`, substituting their own GEF/GTPase/GAP and the specific effectors they activate. Grounded in GO:0007264 (small GTPase-mediated signal transduction).
Reusable conformance target. A node in a concrete pathway declares `conforms_to: [{template: gtpase_switch}]` when its steps instantiate the GEF-load / active-GTPase / GAP-hydrolyze switch. The Ras switch inlined in MODULE:erk_cascade is one realization. Participants are abstract selectors because the motif asserts the switch chemistry only.
All recommended fields populated.
✗ none found
No MODULE:gtpase_switch deep-research report alongside the module YAML.
3 leaf node(s) with no concrete protein grounding:
✓ every declared conforms_to bundle matches its template motif.
No concrete UniProt-grounded genes in this module.
A GEF catalyzes release of GDP and binding of GTP, switching the GTPase on.
Loads GTP onto the GTPase, activating the switch.
The GTP-bound GTPase adopts its active conformation, engages effectors, and possesses intrinsic GTP-hydrolytic activity that resets the switch.
Binary switch; active when GTP-bound, engages effectors.
A GAP accelerates GTP hydrolysis, returning the GTPase to its inactive GDP-bound state.
Stimulates GTP hydrolysis to switch the GTPase off.