In molecular biology, the arfaptin domain is a protein domain which interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules.
The actin cytoskeleton directly determines the morphology of the spine, and actin regulators, small GTPases such as Rac, RhoA, and CDC42, rapidly modify this cytoskeleton.
Once phosphorylated, PKB is in its active form and phosphorylates TBC1D4, which inhibits the GAP domain or the GTPase-activating domain associated with TBC1D4, allowing for Rab protein to change from its GDP to GTP bound state.
RCC1 is the guanine nucletoot change factor for Ran GTPase.
RhoC GTPase is overexpressed, possibly related to overexpression (hypomethylation) of caveolin-1 and -2.
Rabaptin is a 100kDa coiled-coil protein that interacts with the GTP form of the small GTPase Rab5 (see RAB5A, RAB5B, RAB5C) a potent regulator of endocytic transport.
By binding plexin B1 receptor it functions as an R-Ras GTPase-activating protein (GAP) and repels axon growth cones in both the mature central nervous system.
The protein is a Rho GTPase-activating protein (GAP), a type of protein that regulates members of the Rho family of GTPases.
RhoU/Wrch delineates with RhoV/Chp a Rho subclass related to Rac and Cdc42, which emerged in early multicellular organisms during evolution.