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Like most G proteins, RhoA cycles between an inactive GDP-bound form and an active GTP-bound form. Activation is mediated by guanine nucleotide exchange factors (GEFs) that catalyze exchange of GDP for GTP. GTPase activating proteins (GAPs) inactivate RhoA by stimulating intrinsic GTPase activity. GDI sequesters inactive GDP-bound RhoA in the cytoplasm.
