Dynamins are large superfamily GTPase proteins that are involved in various cellular processes including budding of transport vesicles, division of organelles, cytokinesis, and pathogen resistance. Dynamins contain five domains, including GTPase domain, middle domain, PH domain, GTPase effector domain (GED), and proline rich domain (PRD). Importantly, Dynamin is essential for clathrin-coated vesicle formation in endocytosis, in transport from the trans Golgi network, as well as for ligand uptake through caveolae. Furthermore, Dynamin family members also play a role in many processes including division of organelles, cytokinesis and microbial pathogen resistance.

Dynasore is a GTPase activity of dynamin inhibitor, that interferes with the GTPase activity of dynamin1, dynamin2 and Drp1 (mitochondrial dynein) in vitro, but does not interfere with the GTPase activity of other small GTPases. This compound acts as a potent endocytic pathways inhibitor known to depend on dynamin by rapidly blocking coated vesicle formation. Dynasore will not prevent the self-assembly of dynein or its binding to lipids under low ionic strength conditions. Moreover, it is used to capture the intermediate state formed by the pits of the endocytic clathrin coating. In addition, Dynasore also has an antiviral effect, inhibiting HSV-1 and HSV-2 infection of human epithelial and neuronal cells, including primary genital tract cells and human fetal neurons and astrocytes. Further studies have shown that Dynasore does not hinder the nuclear localization of newly synthesized proteins but rather blocks the transport of the proteins out of the nucleus.

To sum up, Dynasore is a dynamin inhibitor, inhibits the GTPase activity of dynamin1, dynamin2 and Drp1.


[1] Eric Macia, et al. Dev Cell. 2006 Jun;10(6):839-50.

[2] Mascha B Mues, et al. J Virol. 2015 Jul;89(13):6673-84.