Dynamin-3 (DNM3)

Dynamin-3 (DNM3) is a member of the dynamin superfamily of large GTPases involved in membrane remodeling, fission, and vesicle formation[1][5][6]. DNM3 possesses a N-terminal GTPase domain, pleckstrin homology (PH) domain for membrane interaction, and a proline/arginine-rich domain (PRD) that serves as a hub for binding SH3 domain-containing proteins[1][2][6]. DNM3 is critical for clathrin-mediated endocytosis, functioning in the scission of vesicles from the plasma membrane and regulating receptor trafficking, especially in neurons where it mediates postsynaptic receptor recycling through interaction with adaptor proteins such as Homer[3]. DNM3 also plays an essential role in megakaryocyte development and platelet biogenesis, influencing progenitor amplification, cytoplasmic enlargement, and demarcation membrane system (DMS) formation[1]. Disruption or knockdown of DNM3 significantly impairs megakaryocyte maturation and can reduce platelet production[1]. While DNM3 is implicated in neurobiology, metabolism, and hematopoiesis, it is not currently the direct target of any approved therapeutic agents and remains primarily a subject of basic and translational research.

Other names

Dynamin-3DNM3KIAA0820Dynamin, testicularT-dynaminDyna IIIdynamin family member

Inhibition of dynamin GTPase activity (experimental compounds only), disruption of vesicle fission and endocytosis