High impact information on Rhog

• Fgd2 identifies a second Rho G protein signaling pathway promoting TRD [1].
• Transient transfection assays in NIH-3T3 cells show that phosphorylated wild-type Vav-2 and the Vav-2 oncoprotein induce cytoskeletal changes resembling those observed by the activation of the RhoG pathway [2].
• Although RhoG deficiency produces a mild phenotype, our experiments suggest that RhoG may contribute to the negative regulation of immune responses [3].
• The lack of a strong phenotype could indicate a functional redundancy of RhoG with other Rac proteins in lymphocytes [3].
• Despite the absence of RhoG, the development of B and T lymphocytes was unaffected [3].

Biological context of Rhog

• Our study indicates that RhoG and Rac1 share overlapping, but not identical, signal transduction pathways [4].
• RESULTS: Expression of Rac1 or RhoG modulated the saturation density to which the cells grew, probably by affecting the level of contact inhibition [5].
• Mastoparan-stimulated insulin secretion was resistant to GGTI-2147, a specific inhibitor of geranylgeranylation of Rho G proteins (e.g. Rac), suggesting that mastoparan induces direct activation of Rac via GTP/GDP exchange [6].

Associations of Rhog with chemical compounds

• Taken together, our findings implicate Rho G proteins, specifically Rac, in mastoparan-induced insulin release [6].
• Dbs is a guanine nucleotide exchange factor which is expressed throughout thymocyte development and is able to activate the Rho family GTPases CDC42, RhoA and RhoG [7].
• These data therefore clarify the role of RhoG in integrin signaling and cell motility [8].

Other interactions of Rhog

• Structural basis for the signaling specificity of RhoG and Rac1 GTPases [4].
• RhoG is a low-molecular-weight GTPase highly expressed in lymphocytes that activates gene transcription and promotes cytoskeletal reorganization in vitro [3].

References