FAM21A Activators

FAM21A, as a component of the WASH complex, plays a crucial role in actin polymerization and cytoskeletal dynamics. Activation of adenylyl cyclase leading to increased cAMP levels can enhance the actin polymerization process that FAM21A regulates. Similarly, stabilization of actin filaments increases actin polymerization, which falls under the regulatory scope of the WASH complex. Phosphorylation by protein kinase C also influences proteins in actin assembly, potentially augmenting FAM21A's contribution to actin dynamics. Additionally, the inhibition of protein phosphatases leads to a rise in phosphorylation of proteins, a modification that can enhance actin cytoskeleton dynamics, in which FAM21A is implicated. The actin nucleation activity of the WASH complex can be augmented by inhibiting specific GTPases, thereby amplifying FAM21A's role in actin filament organization.

Further modulation of FAM21A activity arises from alterations in actin-myosin interactions, as the inhibition of myosin II ATPase activity can indirectly promote FAM21A's function in actin filament elongation. Inhibitors that bind to actin monomers or filaments result in altered actin dynamics, leading to an increased dependence on FAM21A for actin network formation. Inhibition of GSK-3β induces changes in cytoskeletal organization and may upregulate pathways that increase FAM21A activity.