Rheb (Ras homologue enriched in brain) was originally identified as a small guanosine triphosphate (GTP)-binding protein upregulated in the brain in response to electroconvulsive shock (Yamagata et al. 1994). Despite its name, Rheb protein is ubiquitously expressed in a variety of tissues. Rheb is evolutionarily conserved between yeast and humans, and it belongs to the Ras subfamily. In mammals, two different Rheb genes have been identified: Rheb and RhebL (also called Rheb1 and Rheb2, respectively). Since the Rheb GTPase was found to be regulated by the Tsc1 and Tsc2 proteins, which are responsible for the tuberous sclerosis complex (TSC) (Pan et al. 2004), Rheb functions have been extensively investigated. Moreover, Rheb has been demonstrated to activate the mammalian target of rapamycin (mTOR) signaling pathway and to regulate protein translation, cell proliferation, cell size, and metabolism.
Protein and Gene Structure
KeywordsHydrolysis Glycine Proline Arginine Tamoxifen
- Tamai T, Yamaguchi O, Hikoso S, Takeda T, Taneike M, Oka T, et al. Rheb (Ras homologue enriched in brain)-dependent mammalian target of rapamycin complex 1 (mTORC1) activation becomes indispensable for cardiac hypertrophic growth after early postnatal period. J Biol Chem. 2013;288:10176–87. doi:10.1074/jbc.M112.423640.CrossRefPubMedPubMedCentralGoogle Scholar