Diaphanous-related formin 1 (mDia1)

Diaphanous-related formin 1 (mDia1) is a member of the formin protein family and acts as a key regulator of the actin cytoskeleton in eukaryotic cells. It functions as an effector for Rho GTPases and is essential for actin filament nucleation, elongation, and organization. mDia1 forms dimers that processively cap growing actin filaments and is autoinhibited by intramolecular interaction between its N-terminal and C-terminal domains, a process relieved by Rho GTPase binding. Through these activities, mDia1 is critical in cellular processes such as stress fiber and filopodia formation, cytokinesis, cell migration, and cellular response to extracellular signals. It also contributes to phagocytosis and microtubule stabilization, and through regulation of actin dynamics, indirectly modulates transcription via serum response factor (SRF) activation. Dysregulation of mDia1 has implications in cancer and development due to its control of cytoskeletal remodeling and cell movement.

Other names

Dia1Drf1Diaph1KIAA4062p140mDiamKIAA4062D18Wsu154e

Actin nucleation by interaction with barbed ends of actin filaments Relief of autoinhibition through Rho GTPase binding, promoting actin assembly