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Activation and deactivation. Ras is a guanosine - nucleotide -binding protein. Specifically, it is a single-subunit small GTPase, which is related in structure to the G α subunit of heterotrimeric G proteins (large GTPases). G proteins function as binary signaling switches with "on" and "off" states.
The RAS superfamily of GTP (guanosine triphosphate) hydrolysis–coupled signal transduction relay proteins can be subclassified into RAS, RHO, RAB, and ARF families, as well as the closely related Gα family. The members of each family can, in turn, be arranged into evolutionarily conserved branches.
23 de may. de 2023 · Small GTPases including Ras, Rho, Rab, Arf, and Ran are omnipresent molecular switches in regulating key cellular functions. Their dysregulation is a therapeutic target for tumors,...
30 de oct. de 2020 · RAS GTPases are fundamental regulators of development and drivers of an extraordinary number of human cancers. RAS oncoproteins constitutively signal through downstream effector proteins, triggering cancer initiation, progression and metastasis.
Ras-specific GTPase-activating proteins (RasGAPs) down-regulate the biological activity of Ras proteins by accelerating their intrinsic rate of GTP hydrolysis, basically by a transition state stabilizing mechanism.
5 de feb. de 2021 · Ras homology (RHO) GTPases are signalling proteins that have crucial roles in triggering multiple immune functions. Through their interactions with a broad range of effectors and kinases, they...
6 de jun. de 2017 · All four RAS isoforms contain identical residues in the first half of the GTPase domain (G-domain) and they share 82% sequence identity in the second half of the G-domain. The last 19–20 amino acids located at the C-terminal end exhibit significant sequence diversity among RAS isoforms and constitute the “hypervariable region (HVR)”.
