Syne-3 Inhibitors
Chemical inhibitors of Syne-3 target various elements of the cellular cytoskeleton to disrupt the protein's function. Blebbistatin, by selectively inhibiting myosin II ATPase activity, impairs the mechanical forces essential for Syne-3's role in nuclear positioning. Similarly, ML-7, through its inhibition of myosin light chain kinase, blocks the phosphorylation of myosin light chains, which is necessary for myosin motor activity and, by extension, for the functionality of Syne-3. The Rho-associated protein kinase inhibitor Y-27632 impedes the organization of focal adhesions and cytoskeletal structure, thus indirectly hampering the tension and organization that Syne-3 requires to function effectively within the linker of nucleoskeleton and cytoskeleton (LINC) complex.
Further disruption of Syne-3's interaction with the cytoskeleton is achieved with SMIFH2 and CK-636, which inhibit formin-mediated actin polymerization and the actin-nucleating Arp2/3 complex, respectively. These inhibitors lead to a compromised actin cytoskeleton, thereby impacting Syne-3's ability to maintain nuclear architecture. Latrunculin A, by sequestering actin monomers, and Cytochalasin D, by blocking actin polymerization, directly disrupt the actin filaments that Syne-3 associates with. Jasplakinolide, conversely, hyperstabilizes actin filaments, altering the dynamics required for Syne-3's interaction with the cytoskeleton. This alteration hinders the dynamic interaction necessary for Syne-3 to carry out its stabilizing role. Wiskostatin and Swinholide A further contribute to the destabilization of Syne-3 by inhibiting N-WASP and severing actin filaments, respectively, both crucial for the actin dynamics that support Syne-3's function. Mardepodect's inhibition of integrin-extracellular matrix interactions affects the mechanical transduction pathways that Syne-3 is a part of. Lastly, Colchicine, by disrupting microtubule dynamics, indirectly perturbs the actin cytoskeleton and LINC complex, which are essential for the mechanical stability provided by Syne-3.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
(S)-(−)-Blebbistatin | 856925-71-8 | sc-204253 sc-204253A sc-204253B sc-204253C | 1 mg 5 mg 10 mg 25 mg | $71.00 $260.00 $485.00 $949.00 | ||
Blebbistatin is a selective inhibitor of myosin II ATPase activity. Syne-3 is involved in the nuclear envelope, where myosin II has been implicated in the mechanical forces required for proper nuclear positioning. By inhibiting myosin II, Blebbistatin can indirectly impair the proper localization and function of Syne-3. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $89.00 $262.00 | 13 | |
ML-7 is an inhibitor of myosin light chain kinase (MLCK), which phosphorylates myosin light chains, a prerequisite for myosin motor activity. Since Syne-3 association with the cytoskeleton can be affected by myosin dynamics, ML-7's inhibition of MLCK indirectly inhibits Syne-3’s role in linking the cytoskeleton to the nucleus. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $182.00 $693.00 | 88 | |
Y-27632 inhibits ROCK (Rho-associated protein kinase), which is involved in regulating focal adhesion and cytoskeleton organization. As Syne-3 is part of the linker of nucleoskeleton and cytoskeleton (LINC) complex, inhibiting ROCK affects the tension and organization of the cytoskeleton, thereby inhibiting Syne-3 function. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2 inhibits formin-mediated actin polymerization. Since Syne-3 interacts with the actin cytoskeleton, inhibiting formin disrupts actin dynamics and indirectly inhibits the function of Syne-3 in maintaining nuclear architecture and positioning. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $260.00 $799.00 | 36 | |
Latrunculin A binds to actin monomers and prevents their polymerization. Since Syne-3 is linked to actin, the disruption of actin filaments by Latrunculin A would inhibit Syne-3's role in nuclear positioning and integrity. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $180.00 $299.00 | 59 | |
Jasplakinolide stabilizes actin filaments and prevents their disassembly. By hyperstabilizing actin, it can alter the normal dynamics required for Syne-3’s interaction with the cytoskeleton and ultimately inhibit its function. | ||||||
Wiskostatin | 253449-04-6 | sc-204399 sc-204399A sc-204399B sc-204399C | 1 mg 5 mg 25 mg 50 mg | $48.00 $122.00 $432.00 $812.00 | 4 | |
Wiskostatin selectively inhibits the activity of N-WASP, a regulator of actin polymerization via the Arp2/3 complex. Inhibition of N-WASP by Wiskostatin will thus indirectly inhibit the role of Syne-3 in cytoskeletal rearrangements and nuclear positioning. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $145.00 $442.00 | 64 | |
Cytochalasin D binds to the barbed ends of actin filaments, blocking polymerization and elongation. This leads to a disruption of actin filaments, which would inhibit the function of Syne-3 in maintaining the structural integrity of the nucleus. | ||||||
Swinholide A, Theonella swinhoei | 95927-67-6 | sc-205914 | 10 µg | $135.00 | ||
Swinholide A severs actin filaments and prevents their reannealing. By disrupting actin filament integrity, Swinholide A would inhibit the mechanical role of Syne-3 in nuclear positioning and stability. | ||||||
Colchicine | 64-86-8 | sc-203005 sc-203005A sc-203005B sc-203005C sc-203005D sc-203005E | 1 g 5 g 50 g 100 g 500 g 1 kg | $98.00 $315.00 $2244.00 $4396.00 $17850.00 $34068.00 | 3 | |
Colchicine binds to tubulin and inhibits its polymerization, disrupting microtubule dynamics. Although primarily affecting microtubules, this disruption can have downstream effects on the actin cytoskeleton and the LINC complex, thereby indirectly inhibiting Syne-3 function. | ||||||