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Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. Additionally we are shipping Ras-Related GTP Binding B Antibodies (43) and and many more products for this protein.
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Data suggest DNM2 (show DNM2 Proteins)/RRAGB- (or DNM2 (show DNM2 Proteins)/RRAGC (show RRAGC Proteins)-)dependent endocytosis of extracellular amino acids (AAs (show FGD1 Proteins)) plays critical role in mTORC1 transport/activation; recruitment of mTORC1 from cytoplasm to lysosome is suppressed by DNM2 (show DNM2 Proteins) inhibition; AA deprivation appears to be main cause of mTORC1 inactivation via DNM2 (show DNM2 Proteins) inhibition. (RHEB (show RHEB Proteins) = Ras homolog enriched in brain (show RHEB Proteins); DNM2 (show DNM2 Proteins) = dynamin II (show DNM2 Proteins); RRAG = Ras-related GTP binding protein (show RAB10 Proteins))
Inhibition of glutaminolysis prevents GTP (show AK3 Proteins) loading of RagB and lysosomal translocation and subsequent activation of mTORC1.
RagA (show RRAGA Proteins) and RagB are key regulators of lysosomal function and cardiac protection.
Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. These proteins represent cellular switches that are operated by GTP-exchange factors and factors that stimulate their intrinsic GTPase activity. All GTPases of the Ras superfamily have in common the presence of six conserved motifs involved in GTP/GDP binding, three of which are phosphate-/magnesium-binding sites (PM1-PM3) and three of which are guanine nucleotide-binding sites (G1-G3). Transcript variants encoding distinct isoforms have been identified.
GTP-binding protein ragB
, rag B
, ras-related GTP-binding protein B
, Ras-related GTP binding B