 RhoA is sequestered by dissociation inhibitors (RhoGDIs) which remove the protein from the membrane while preventing its further interaction with other downstream effectors.RhoA acquires both inactive GDP-bound and active GTP-bound conformational states; these states alternate between the active and inactive states via the exchange of GDP to GTP (conducted simultaneously via guanine nucleotide exchange factors and GTPase activating factor).RhoA is activated primarily by guanine nucleotide exchange factors (GEFs) via phosphorylation; due to large network of overlapping phosphorylation, a multitude of GEFs are utilized to enable specific signaling pathways.