epsin Activators
Epsin Activators encompass a diverse array of chemical compounds that indirectly enhance the functional activity of epsin, predominantly through modulation of endocytic pathways and membrane dynamics. Phosphatidylinositol 4,5-bisphosphate (PIP2) directly binds to the epsin N-terminal homology (ENTH) domain, a critical interaction for inducing membrane curvature and promoting clathrin-mediated endocytosis, which is a primary function of epsin. Similarly, echistatin, by inhibiting integrin functions, may relieve epsin of competitive cellular processes, allowing for heightened endocytic activity. Dynasore, through its inhibitory action on dynamin, results in an accumulation of clathrin-coated pits, which could lead to an increased demand for epsin's role in vesicle formation and scission. Actin dynamics are crucial in endocytosis, and compounds like phalloidin and jasplakinolide, by stabilizing F-actin, likely enhance the efficiency of epsin's involvement in this process. Chlorpromazine, by dispersing clathrin, may enhance epsin activity by increasing the pool of clathrin available for pit formation. Piperine, by modulating membrane lipids, creates a favorable environment for epsin-mediated membrane invagination, while neomycin changes membrane curvature to potentially facilitate epsin's role in endocytosis initiation.
The activity of epsin is further influenced by chemicals that modulate the membrane structure and intracellular signaling pathways. Okadaic acid maintains the phosphorylation state of proteins involved in endocytosis, potentially shifting the cellular equilibrium to favor epsin-mediated vesicle formation. Nystatin and filipin, by binding to components in the membrane, induce changes that could prompt the cell to engage in compensatory endocytosis, potentially increasing the functional demand on epsin. Moreover, alterations in the lipid raft composition by filipin may enhance epsin's ability to induce membrane curvature and facilitate vesicle budding. These epsin activators, through their targeted effects on cellular structures and signaling, collectively enhance the formation of clathrin-coated vesicles and the overall endocytic machinery in which epsin is a key component, without the need to directly upregulate its expression or activity.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Dynamin Inhibitor I, Dynasore | 304448-55-3 | sc-202592 | 10 mg | $87.00 | 44 | |
Dynasore is a small molecule that inhibits the GTPase activity of dynamin, a protein involved in the final scission of clathrin-coated pits during endocytosis. Inhibition of dynamin function can lead to an accumulation of clathrin-coated pits, which may indirectly increase the demand for epsin's endocytic role, thereby enhancing its activity. | ||||||
Phalloidin | 17466-45-4 | sc-202763 | 1 mg | $229.00 | 33 | |
Phalloidin stabilizes F-actin filaments and could potentiate epsin's role in endocytosis. The actin cytoskeleton is known to play a role in the formation of clathrin-coated pits, and by stabilizing actin filaments, phalloidin may increase the efficiency of epsin-mediated membrane invagination and internalization. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $180.00 $299.00 | 59 | |
Jasplakinolide is a cyclodepsipeptide that also stabilizes actin filaments, similar to phalloidin. By promoting actin polymerization, it can potentiate epsin's interaction with the plasma membrane and clathrin-coated vesicles, enhancing the endocytic process that epsin is involved in. | ||||||
Chlorpromazine | 50-53-3 | sc-357313 sc-357313A | 5 g 25 g | $60.00 $108.00 | 21 | |
Chlorpromazine is known to disrupt clathrin-mediated endocytosis by dispersing clathrin and adaptor proteins from the plasma membrane. This disruption could indirectly enhance epsin's activity by increasing the pool of available clathrin and adaptor proteins for epsin-mediated assembly of clathrin-coated pits. | ||||||
Piperine | 94-62-2 | sc-205809 sc-205809A | 5 g 25 g | $36.00 $143.00 | 3 | |
Piperine has been shown to interfere with endocytic pathways by modulating membrane lipids and influencing the fluidity and curvature of the membrane. This could enhance epsin's functional activity by creating an environment that is more conducive to the membrane deformation and invagination that epsin promotes during clathrin-mediated endocytosis. | ||||||
Neomycin sulfate | 1405-10-3 | sc-3573 sc-3573A | 1 g 5 g | $26.00 $34.00 | 20 | |
Neomycin binds to phospholipids, particularly phosphatidylinositol phosphates, and can change membrane curvature. This alteration in membrane topology can enhance epsin's activity by facilitating its role in membrane deformation during the initiation of endocytosis. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
Okadaic acid is a potent inhibitor of protein phosphatases 1 and 2A, which can regulate dephosphorylation of proteins involved in endocytosis. By inhibiting these phosphatases, okadaic acid could indirectly enhance epsin-mediated endocytosis by maintaining the phosphorylation state of proteins that promote clathrin-coated pit formation and vesicle scission. | ||||||
Nystatin | 1400-61-9 | sc-212431 sc-212431A sc-212431B sc-212431C | 5 MU 25 MU 250 MU 5000 MU | $50.00 $126.00 $246.00 $3500.00 | 7 | |
Nystatin binds to ergosterol in membranes, creating pores that disrupt normal membrane function. This disruption can potentially enhance the functional activity of epsin by inducing compensatory endocytic mechanisms to remove the damaged portions of the plasma membrane. | ||||||