CapZ-α Inhibitors
Chemical classes known as CapZ-α inhibitors encompass compounds that influence actin dynamics, which can indirectly affect the function of CapZ-α. CapZ-α is pivotal in capping the barbed ends of actin filaments, an action essential for regulating actin polymerization and maintaining cellular structural integrity. The inhibitors listed, while not targeting CapZ-α directly, exert their effects through modulation of actin filament assembly, stability, or interactions with other actin-binding proteins. For instance, cytochalasin D and latrunculin A bind directly to actin filaments and monomers, respectively, disrupting the polymerization process and potentially reducing the need for CapZ-α activity. Swinholide A, by severing actin filaments, and jasplakinolide, through filament stabilization, alter the equilibrium of actin polymerization and depolymerization, impacting CapZ-α function.
CapZ-α inhibitors target actin nucleators such as the Arp2/3 complex and formins, thus indirectly influencing the formation of new actin filaments that CapZ-α would cap. Similarly, inhibitors of proteins that regulate actin dynamics target MLCK and ROCK respectively, as well as blebbistatin, an inhibitor of myosin II, can modify the actin cytoskeleton. These alterations can change the cellular requirements for CapZ-α-mediated capping. These compounds collectively modulate the actin cytoskeleton, thereby indirectly influencing the functionality of CapZ-α without directly binding to or altering the protein itself. The interactions of these chemicals with actin dynamics offer insights into the indirect regulation of CapZ-α activity and underscore the complexity of targeting specific protein functions through the actin cytoskeleton network.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D binds to the growing ends of actin filaments, preventing further polymerization and leading to depolymerization. Although it does not target CapZ-α directly, by capping the barbed end, it can mimic the function of CapZ-α, thus potentially competing with it and indirectly decreasing its capping activity on new filaments. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A binds to monomeric G-actin, sequestering it and preventing its polymerization into F-actin. With less G-actin available for filament elongation, CapZ-α's role in capping the barbed ends of actin filaments can be indirectly affected as there are fewer filaments requiring capping. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Jasplakinolide stabilizes actin filaments and promotes their assembly. It does not directly inhibit CapZ-α, but by stabilizing filaments, it may reduce the turnover rate of actin filament ends, thus potentially reducing the need for CapZ-α's capping function. | ||||||
Phalloidin | 17466-45-4 | sc-202763 | 1 mg | $234.00 | 33 | |
Phalloidin binds and stabilizes F-actin, preventing filament depolymerization. While not a direct inhibitor of CapZ-α, the stabilization of actin filaments can reduce the dynamic range within which CapZ-α operates, as fewer free barbed ends would be available for capping. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $91.00 $267.00 | 13 | |
ML-7 is an inhibitor of myosin light chain kinase (MLCK). It affects actin-myosin contractility and can indirectly influence the tension and dynamics of actin filaments, which may alter the requirements for CapZ-α capping activity. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $186.00 $707.00 | 88 | |
Y-27632 is an inhibitor of Rho-associated protein kinase (ROCK), which plays a role in actin cytoskeleton organization. By inhibiting ROCK, Y-27632 can lead to changes in actin dynamics and potentially reduce the cellular need for CapZ-α's action. | ||||||
(S)-(−)-Blebbistatin | 856925-71-8 | sc-204253 sc-204253A sc-204253B sc-204253C | 1 mg 5 mg 10 mg 25 mg | $72.00 $265.00 $495.00 $968.00 | ||
Blebbistatin is an inhibitor of myosin II and affects muscle contraction and cell motility by interfering with the myosin-actin interaction. Reduction in actin-myosin interactions can lead to changes in actin filament dynamics, which could indirectly influence CapZ-α activity. | ||||||
BEZ235 | 915019-65-7 | sc-364429 | 50 mg | $211.00 | 8 | |
SMIFH2 is an inhibitor of the formin family of proteins, which are involved in actin nucleation and elongation. Inhibition of formin can lead to a decrease in filament elongation, which may reduce the requirement for CapZ-α's capping function. | ||||||