Syne-4 Inhibitors
Syne-4 inhibitors are a class of compounds that specifically target and inhibit the function of Syne-4, a member of the spectrin repeat-containing nuclear envelope (Syne) family of proteins. Syne-4, also known as Nesprin-4, is a key component of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex, which connects the cytoskeleton to the nuclear envelope. Syne-4 primarily interacts with microtubule motors, particularly kinesin-1, facilitating the positioning of the nucleus within the cell by linking the cytoskeleton to the outer nuclear membrane. This function is essential for maintaining cellular structure, nuclear migration, and proper intracellular communication between the cytoskeleton and the nucleus. Inhibitors of Syne-4 interfere with these protein interactions, disrupting the physical connection between the cytoskeleton and the nuclear envelope, which can lead to alterations in nuclear positioning and cytoskeletal dynamics.
The chemical nature of Syne-4 inhibitors is diverse, reflecting various mechanisms of action. Some inhibitors may directly bind to the spectrin repeats of Syne-4, preventing it from engaging with kinesin or other motor proteins involved in nuclear positioning. Others may act by altering the conformational structure of Syne-4, reducing its ability to participate in the LINC complex and disrupt its function in nuclear anchoring. By inhibiting Syne-4, these compounds can interfere with key processes like nuclear migration, cellular polarity, and mechanical force transmission across the nuclear envelope. Understanding how Syne-4 inhibitors function provides important insights into the molecular mechanisms governing cell architecture and intracellular organization, as well as the broader role of the LINC complex in maintaining cellular integrity. This knowledge expands our understanding of how cells maintain spatial organization and respond to mechanical signals within their environment.
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| 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 | $72.00 $265.00 $495.00 $968.00 | ||
Blebbistatin inhibits myosin II ATPase activity, which can lead to a reduction in myosin II-driven contractility within cells. As Syne-4 is implicated in linking the actin cytoskeleton to the nuclear envelope, blebbistatin's inhibition of myosin II can impact Syne-4's ability to maintain these connections by altering cytoskeletal dynamics. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $91.00 $267.00 | 13 | |
ML-7 inhibits myosin light chain kinase, which phosphorylates myosin light chains, a crucial step for actin-myosin contraction. Inhibition of this kinase can therefore decrease actomyosin contractility, which can disrupt the mechanical stability that Syne-4 relies on to connect the cytoskeleton to the nuclear membrane. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A binds to actin monomers and prevents their polymerization. Syne-4, which associates with actin filaments, can be functionally inhibited by the prevention of actin filament formation, leading to a compromised cytoskeletal framework. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D disrupts actin polymerization and can also induce filament depolymerization. By destabilizing actin filaments, it can inhibit Syne-4's functionality, as Syne-4 is dependent on intact actin filaments to perform its structural role at the nuclear envelope. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $186.00 $707.00 | 88 | |
Y-27632 is a ROCK inhibitor which affects actin cytoskeletal organization by reducing the phosphorylation of downstream targets necessary for stress fiber formation. Syne-4's function can be inhibited by Y-27632 due to alterations in the actin cytoskeleton that compromise Syne-4's structural support role. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Jasplakinolide stabilizes actin filaments, and while it does not depolymerize actin, it can inhibit the dynamic rearrangement of the actin cytoskeleton. This stabilization can inhibit Syne-4 function by locking actin structures in a state that is not conducive to Syne-4's role in maintaining dynamic connections between the cytoskeleton and nuclear envelope. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2 inhibits formin-mediated actin assembly, which is critical for the formation of long actin filaments. By inhibiting formin activity, SMIFH2 can impair the actin filament elongation that Syne-4 depends on for its role in linking the nucleus with the cytoskeleton. | ||||||
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 | $100.00 $321.00 $2289.00 $4484.00 $18207.00 $34749.00 | 3 | |
Colchicine binds to tubulin and inhibits microtubule polymerization, which can affect cellular mechanics and the integrity of the cytoskeleton. By disrupting microtubules, colchicine can indirectly inhibit Syne-4 by altering the cytoskeletal network that supports Syne-4's function. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $59.00 $85.00 $143.00 $247.00 | 38 | |
Nocodazole disrupts microtubule dynamics by inhibiting their polymerization. This disruption can lead to an indirect inhibition of Syne-4 by affecting the structural integrity of the cytoskeleton and thus Syne-4's role in maintaining nuclear-cytoskeletal linkages. | ||||||
Taxol | 33069-62-4 | sc-201439D sc-201439 sc-201439A sc-201439E sc-201439B sc-201439C | 1 mg 5 mg 25 mg 100 mg 250 mg 1 g | $41.00 $74.00 $221.00 $247.00 $738.00 $1220.00 | 39 | |
Paclitaxel stabilizes microtubules and prevents their disassembly. This stabilization can indirectly inhibit Syne-4 by altering the dynamics and organization of the cytoskeleton, potentially impacting Syne-4's ability to functionally interact with the nuclear envelope. | ||||||