Open in a separate window. Table 1 Evidence supporting dynamin-dependent and dynamin-independent effects of dynasore. In the Golgi, SREBP-2 is cleaved to release the active form, which enters the nucleus and drives transcription of genes encoding most components of the mevalonate pathway, and for the LDLR. I Martin Sheldon, Email: Support Center Support Center.

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The stages of clathrin-coated vesicle formation. Lipid rafts contribute to the compartmentalization of membranes and the spatiotemporal regulation of cellular signalling. Support Center Support Center.

On the other hand, many pathogens have evolved to exploit endocytosis to enter eukaryotic cells. Dynasore, a dynamin inhibitor, suppresses lamellipodia formation and cancer cell invasion by destabilizing actin filaments.

Macropinocytosis, unlike clathrin-mediated endocytosis, is a dynamin-independent processes [ 35 ]. In Drosophila melanogaster and Caenorhabditis elegans only one dynamin isoform has been identified [ 15 – 17 ].

Dynasore, a cell-permeable inhibitor of dynamin.

It would be interesting for future work dynqsore explore if dynasore impacts not only labile cholesterol in plasma membranes, but also the sphyngomyelin-bound cholesterol in lipid rafts.


Biochem Biophys Res Commun. Domain structure and intramolecular regulation of dynamin GTPase. In the Golgi, SREBP-2 is cleaved to release the active form, which enters the nucleus and drives transcription of genes encoding most components of the mevalonate pathway, and for the LDLR.

Dynasore – not just a dynamin inhibitor

Dynamin triple knockout cells reveal off target effects of commonly used dynamin inhibitors. Taking the above findings together, one inference is that cells deficient in dynamin or treated with dynasore would not initiate mechanisms to increase cellular cholesterol when cholesterol is depleted in different compartments, because the ER contains surplus free cholesterol.

National Center dynasorr Biotechnology InformationU. Dynasore, a cell-permeable inhibitor of dynamin. Recent evidence supports a concept for three pools of cholesterol in plasma membranes [ 28 ]: D Dynasore, perhaps by remodelling actin filaments, as well dynasord reducing plasma membrane cholesterol, disperses the organization of lipids in lipid rafts.

Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic. These limitations of dynasore lead to the synthesis of dihydroxyl dynawore trihydroxyl dynasore analogs, called the Dyngo compounds, which have improved potency, reduced cytotoxicity, and reduced detergent binding [ 26 ].

Differential endometrial cell sensitivity to xynasore cholesterol-dependent cytolysin links Trueperella pyogenes to uterine disease in cattle. Dynasore inhibits the GTPase activity of dynamin, blocking constriction and fission. Nat Rev Mol Cell Biol. As well as effects on cellular cholesterol attributable to inhibition of dynamin, recent observations imply that dynasore also influences cholesterol homeostasis in a dynamin-independent manner.


Dynasore, a cell-permeable inhibitor of dynamin.

As well as linking to the actin cytoskeleton during clathrin-coated vesicle formation, interaction between dynamin and the actin cytoskeleton occurs during the formation of membrane ruffles, lamellapodia, and podosomes [ 4 – 6 ]. Received Feb 4; Accepted Mar Am J Physiol Cell Physiol. However, other cholesterol-dependent cytolysins, such as Perfringolysin O, bind the labile cholesterol in cellular membranes [ 28 ].

Dynamin and its role in membrane fission. Dynamin is an intracellular protein with essential roles in membrane remodelling and fission of clathrin-coated vesicles formed during endocytosis, and vesicles that bud from the trans-Golgi network [ 1 ].

Simons K, Ikonen E. The implication of this observation is that dynasore treatment would then lead to depletion of labile cholesterol in the plasma membrane. Indeed, dynasore destabilizes and remodels F-actin in vitro [ 5152 ]. James G Cronin, Email: Eur J Cell Biol. I Martin Sheldon, Email: Functional rafts in cell membranes.

Golgi vesiculation induced by cholesterol occurs by a dynamin- and cPLA2-dependent mechanism.