Myosin VI Activators
The chemical class of Myosin VI activators comprises a diverse array of compounds that modulate Myosin VI activity directly or indirectly, emphasizing the intricate regulation of this motor protein within the cellular context. These activators offer insights into the complex interplay between actin dynamics and Myosin VI function, providing potential strategies for manipulating Myosin VI activity in a controlled manner. CK-666 and its analog, along with CK-869, act as indirect activators by inhibiting the Arp2/3 complex, disrupting actin nucleation, and remodeling. This alteration in actin dynamics creates a permissive environment for Myosin VI binding and movement, showcasing the interconnected regulation of actin-associated molecular motors and the modulation of Myosin VI activity. Blebbistatin and its analog, as well as Y-27632, H-1152, and Thiazovivin, act as indirect activators by modulating actin-myosin interactions through the inhibition of myosin II or ROCK. These compounds reduce myosin II-mediated contractility, altering actin-myosin dynamics and relieving inhibitory forces on Myosin VI. The indirect activation highlights the intricate regulatory network governing cellular tension and contractility and its impact on Myosin VI activity.
Jasplakinolide and Latrunculin A indirectly activate Myosin VI by influencing actin polymerization dynamics. Jasplakinolide stabilizes actin filaments, promoting the formation of actin bundles, while Latrunculin A disrupts actin polymerization by sequestering actin monomers. Both compounds create a permissive environment for Myosin VI binding and movement, demonstrating unique strategies for indirectly modulating Myosin VI by targeting specific aspects of actin dynamics. Blebbistatin Analog, SMIFH2, and the CK-666 Analog showcase alternative approaches to indirect activation by influencing actomyosin contractility and formin-mediated actin polymerization, respectively. These compounds provide additional insights into the diverse mechanisms that can be exploited to regulate Myosin VI activity indirectly.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
CK 666 | 442633-00-3 | sc-361151 sc-361151A | 10 mg 50 mg | $321.00 $1040.00 | 5 | |
CK-666, a small molecule, acts as an indirect activator of Myosin VI by influencing actin dynamics. It inhibits the Arp2/3 complex, preventing the nucleation of actin filaments. The reduction in branched actin structures alters the actin cytoskeleton architecture, leading to increased Myosin VI activity. | ||||||
(±)-Blebbistatin | 674289-55-5 | sc-203532B sc-203532 sc-203532A sc-203532C sc-203532D | 5 mg 10 mg 25 mg 50 mg 100 mg | $183.00 $313.00 $464.00 $942.00 $1723.00 | 7 | |
Blebbistatin, a small molecule inhibitor of non-muscle myosin II, serves as an indirect activator of Myosin VI by modulating actomyosin contractility. It reduces myosin II-mediated tension on actin filaments, influencing the overall cellular tension balance. The decreased contractility relieves inhibitory mechanical forces on Myosin VI, allowing for enhanced motor activity. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $186.00 $707.00 | 88 | |
Y-27632, a selective inhibitor of Rho-associated protein kinase (ROCK), acts as an indirect activator of Myosin VI by modulating actin-myosin interactions. It inhibits ROCK, leading to reduced myosin II-mediated phosphorylation of myosin light chain (MLC). The decreased MLC phosphorylation alters actin-myosin contractility, indirectly promoting Myosin VI activity. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Jasplakinolide, a natural cyclic peptide, serves as an indirect activator of Myosin VI by affecting actin polymerization. It stabilizes actin filaments and promotes the formation of actin bundles. The altered actin cytoskeleton enhances the substrate for Myosin VI binding and movement. | ||||||
CK-869 | 388592-44-7 | sc-507274 | 5 mg | $163.00 | ||
CK-869, a potent Arp2/3 complex inhibitor, serves as an indirect activator of Myosin VI by disrupting actin nucleation and remodeling. It inhibits Arp2/3, preventing the formation of branched actin networks. The altered actin dynamics create a permissive environment for Myosin VI binding and movement. | ||||||
H-1152 dihydrochloride | 451462-58-1 | sc-203592 sc-203592A | 1 mg 5 mg | $104.00 $364.00 | 7 | |
H-1152, a selective ROCK inhibitor, acts as an indirect activator of Myosin VI by modulating actin-myosin interactions. It inhibits ROCK, leading to decreased MLC phosphorylation and altered actin-myosin contractility. The indirect activation of Myosin VI by H-1152 underscores the intricate regulatory network governing actin-myosin dynamics, providing a potential avenue for modulating Myosin VI activity by targeting key signaling nodes involved in actomyosin contractility. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A, a marine toxin, serves as an indirect activator of Myosin VI by disrupting actin polymerization. It sequesters actin monomers, preventing their incorporation into growing filaments. The depolymerized actin cytoskeleton creates a permissive environment for Myosin VI binding and movement. | ||||||
Thiazovivin | 1226056-71-8 | sc-361380 sc-361380A | 10 mg 25 mg | $284.00 $634.00 | 15 | |
Thiazovivin, an inhibitor of Rho-associated protein kinase (ROCK), serves as an indirect activator of Myosin VI by modulating actin-myosin interactions. It inhibits ROCK, leading to reduced MLC phosphorylation and altered actin-myosin contractility. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2, a small molecule inhibitor of formin proteins, acts as an indirect activator of Myosin VI by influencing actin dynamics. It inhibits formin-mediated actin polymerization, reducing the formation of linear actin filaments. The altered actin cytoskeleton enhances the substrate for Myosin VI binding and movement. | ||||||