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Guanine nucleotide exchange factor activating the small GTPase RHOA, which, in turn, induces myosin filament formation. Additionally we are shipping PLEKHG6 Antibodies (51) and many more products for this protein.
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Intramolecular interactions between MyoGEF domains act as an autoinhibitory mechanism for the regulation of MyoGEF functions.
Taken together, these results suggest that aurora B (show AURKB Proteins) coordinates with Plk1 to regulate MyoGEF activation and localization, thus contributing to the regulation of cytokinesis.
GIPC1 (show GIPC1 Proteins)-MyoGEF complex formation plays an important role in regulating MDA-MB-231 breast cancer cell polarization and invasion.
ezrin (show EZR Proteins) allows the local activation of RhoG (show RHOG Proteins) at the apical pole of epithelial cells by recruiting upstream and downstream regulators of RhoG (show RHOG Proteins) and that both PLEKHG6 and ezrin (show EZR Proteins) are required for efficient macropinocytosis
Plk1 can regulate MyoGEF activity and localization, contributing to the regulation of cytokinesis
MyoGEF cooperates with nonmuscle myosin IIA to regulate the polarity and invasion activity of breast cancer cells through activation of RhoA (show RHOA Proteins) and RhoC (show RHOC Proteins).
Guanine nucleotide exchange factor activating the small GTPase RHOA, which, in turn, induces myosin filament formation. Also activates RHOG. Does not activate RAC1, or to a much lower extent than RHOA and RHOG. Part of a functional unit, involving PLEKHG6, MYH10 and RHOA, at the cleavage furrow to advance furrow ingression during cytokinesis. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with EZR, required for normal macropinocytosis.
PH domain-containing family G member 6
, myosin interacting guanine nucleotide exchange factor
, myosin-interacting guanine nucleotide exchange factor
, pleckstrin homology domain-containing family G member 6