Sec31B Inhibitors
Chemical inhibitors of Sec31B can impede the protein's function through various mechanisms related to the trafficking and formation of vesicles within the cell. Brefeldin A, for example, directly interferes with the vesicle formation from the ER and Golgi by inhibiting the ARF GTPase, leading to the disassembly of the COPII coat where Sec31B is active, thus impairing its function. Similarly, Gossypol's inhibition of kinases can affect the phosphorylation state of proteins interacting with Sec31B, potentially disrupting the assembly of the COPII complex. Dynasore targets the GTPase dynamin, involved in vesicle scission, indirectly impacting Sec31B's role in vesicle trafficking by disrupting the process of vesicle release. Exo1, by inhibiting the exocyst complex, can affect vesicle docking and fusion, processes that are critical for normal Sec31B function in directing vesicular traffic.
Furthermore, Tunicamycin's inhibition of N-linked glycosylation can lead to an accumulation of misfolded proteins in the ER, which indirectly interferes with Sec31B by overwhelming the protein trafficking machinery. Monensin disrupts the ion gradients across the Golgi membrane, which can lead to protein processing and trafficking defects, thereby functionally inhibiting Sec31B. The role of Sec31B in vesicle trafficking is further compromised by Nocodazole and Cytochalasin D, which disrupt microtubules and actin filaments, respectively, both essential components of the cellular cytoskeleton used for vesicle transport. Latrunculin A, by inhibiting actin polymerization, can disrupt the cytoskeletal dynamics, which in turn can impair the transport of vesicles where Sec31B functions. H-89, though primarily a kinase inhibitor, also inhibits Sar1, which is required for COPII vesicle formation, thus directly affecting Sec31B's role in the process. Ilimaquinone, which disrupts Golgi apparatus function, and Retro-2, which inhibits retrograde transport from the Golgi to the ER, both can lead to a functional inhibition of Sec31B by disrupting the formation and recycling of vesicles essential for its activity. Each of these chemical inhibitors, through their unique action on cellular processes, can lead to an inhibition of Sec31B, demonstrating the protein's integral role in maintaining efficient intracellular transport and vesicle dynamics.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Brefeldin A | 20350-15-6 | sc-200861C sc-200861 sc-200861A sc-200861B | 1 mg 5 mg 25 mg 100 mg | $31.00 $53.00 $124.00 $374.00 | 25 | |
Brefeldin A inhibits ADP-ribosylation factor (ARF), a small GTPase involved in vesicle formation from the ER and Golgi. Since Sec31B is part of the COPII complex involved in ER to Golgi transport, inhibition of ARF by Brefeldin A leads to disassembly of the COPII coat, thereby functionally inhibiting Sec31B. | ||||||
Gossypol | 303-45-7 | sc-200501 sc-200501A | 25 mg 100 mg | $116.00 $230.00 | 12 | |
Gossypol inhibits several enzymes, including kinases, which could be crucial for the phosphorylation state of proteins that interact with Sec31B. This inhibition can impair the formation of the COPII complex where Sec31B operates, leading to its functional inhibition. | ||||||
Dynamin Inhibitor I, Dynasore | 304448-55-3 | sc-202592 | 10 mg | $89.00 | 44 | |
Dynasore is a GTPase inhibitor that targets dynamin, which is involved in vesicle scission. As Sec31B is crucial for vesicle formation, inhibiting dynamin function can disrupt vesicle scission indirectly inhibiting the function of Sec31B in vesicle trafficking. | ||||||
Exo1 | 461681-88-9 | sc-200752 sc-200752A | 10 mg 50 mg | $84.00 $297.00 | 4 | |
Exo1 is a small molecule inhibitor of the exocyst complex, which is involved in vesicle targeting to membranes. Inhibition of the exocyst complex can disrupt vesicle transport and docking, indirectly inhibiting Sec31B's function in vesicle formation and trafficking. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $172.00 $305.00 | 66 | |
Tunicamycin inhibits N-linked glycosylation, which is essential for the proper folding and function of many membrane-bound and secreted proteins. As Sec31B is involved in the trafficking of such proteins, inhibition of glycosylation can lead to a buildup of misfolded proteins, indirectly inhibiting Sec31B function. | ||||||
Monensin A | 17090-79-8 | sc-362032 sc-362032A | 5 mg 25 mg | $155.00 $525.00 | ||
Monensin is an ionophore that disrupts ionic gradients across the Golgi membrane, affecting protein processing and trafficking. Since Sec31B is involved in protein trafficking, the action of Monensin can lead to a functional inhibition of Sec31B by disrupting the environment it operates in. | ||||||
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 microtubules, which are necessary for vesicle transport within the cell. By destabilizing microtubules, Nocodazole can indirectly inhibit Sec31B function by preventing the transport of COPII vesicles along the cytoskeleton. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D inhibits actin polymerization, which can affect vesicle movement and secretion. Sec31B, being involved in vesicle trafficking, can be functionally inhibited by the disruption of actin filaments, affecting the mechanics of vesicle transport. | ||||||
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 inhibits their polymerization, disrupting cytoskeletal dynamics. Since the cytoskeleton is involved in transporting vesicles where Sec31B functions, Latrunculin A can indirectly inhibit the function of Sec31B by impairing vesicle transport. | ||||||
H-89 dihydrochloride | 130964-39-5 | sc-3537 sc-3537A | 1 mg 10 mg | $94.00 $186.00 | 71 | |
H-89 is a kinase inhibitor that also inhibits the activation of Sar1, a small GTPase required for COPII vesicle formation. Inhibiting Sar1 can impair the assembly of the COPII complex, leading to functional inhibition of Sec31B as it is a part of this complex. | ||||||