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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | The Rnd proteins, which form a distinct sub-group of the Rho family of small GTP-binding proteins, have been shown to regulate the organization of the actin cytoskeleton in several tissues [ ]. RhoN (also known as Rnd2 or Rho7) is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd3/RhoE/Rho8. Unlike other small G proteins, Rnd2/RhoN, Rnd3/RhoE, and Rnd1/Rho6 and do not hydrolyze GTP []. This is due to changes in key amino acids involved in catalysing GTP hydrolysis [].Rnd2/RhoN is transiently expressed in radially migrating cells in the brain while they are within the subventricular zone of the hippocampus and cerebral cortex. These migrating cells typically develop into pyramidal neurons. Cells that exogenously expressed Rnd2/RhoN failed to migrate to upper layers of the brain, suggesting that Rnd2/RhoN plays a role in the radial migration and morphological changes of developing pyramidal neurons, and that Rnd2/RhoN degradation is necessary for proper cellular migration. The Rnd2/RhoN GEF Rapostlin is found primarily in the brain and together with Rnd2/RhoN induces dendrite branching [ , ]. Unlike Rnd1/Rho6 and Rnd3/RhoE/Rho8, which are RhoA antagonists, Rnd2/RhoN binds the GEF Pragmin and significantly stimulates RhoA activity and Rho-A mediated cell contraction []. Rnd2/RhoN is also found to be expressed in spermatocytes and early spermatids, with male-germ-cell Rac GTPase-activating protein (MgcRacGAP), where it localizes to the Golgi-derived pro-acrosomal vesicle []. | Name | Rho-related GTP-binding protein RhoN |
| Short Name | RhoN | Type | Family |
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