COPZ Inhibitors
Chemical inhibitors of COPZ employ a variety of mechanisms to disrupt its function, which is essential for vesicular trafficking within cells. Benzyl isothiocyanate targets COPZ by alkylating its cysteine residues, which are crucial for the protein's ability to bind and interact with other proteins, leading to an impairment of its function. Withaferin A, on the other hand, interferes with COPZ by binding to annexin II, a protein that normally interacts with COPZ to form a complex necessary for COPZ's role in vesicle trafficking. This disruption prevents the proper functioning of COPZ in the cellular transport pathways. Similarly, Wiskostatin inhibits the activity of N-WASP, a regulatory protein that controls actin polymerization-a process integral to vesicle movement. Since COPZ is involved in vesicle formation and transport, the inhibition of N-WASP can lead to the impairment of these processes.
Other inhibitors like ML141 and Dynasore directly affect the cytoskeletal dynamics and vesicle scission events, respectively, which are important for COPZ function. ML141 selectively inhibits Cdc42, a GTPase involved in cytoskeletal organization, which can affect the ability of COPZ to participate in vesicle trafficking. Dynasore targets dynamin, another GTPase that plays a pivotal role in the scission of clathrin-coated vesicles from the membrane, and its inhibition can disrupt the function of COPZ by hindering vesicle scission. MiTMAB and Chlorpromazine also inhibit dynamin, but MiTMAB does so by preventing its binding to phospholipids, while Chlorpromazine disassembles clathrin lattices on vesicles, both leading to an indirect inhibition of COPZ by disrupting the vesicle formation and transport processes. Brefeldin A adds another layer of inhibition by disrupting the Golgi apparatus through its action on ADP-ribosylation factor proteins, which are necessary for the formation of COPI vesicles where COPZ operates. Moreover, compounds like Exo2 and SecinH3 exert their effects on the exocyst complex and ARF GTPases, respectively, leading to a disruption in vesicle trafficking and docking processes that are crucial for COPZ activity. Finally, inhibitors like Pitstop 2 targets clathrin-mediated endocytosis, which, while not directly related to COPI vesicles, can still impact COPZ function due to the interconnected nature of vesicular transport pathways. These chemical inhibitors, through their diverse mechanisms, can significantly impede the functioning of COPZ within the cell.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Benzyl isothiocyanate | 622-78-6 | sc-204641 sc-204641A | 5 g 25 g | $46.00 $153.00 | 1 | |
Benzyl isothiocyanate can inhibit COPZ by alkylating cysteine residues that are critical for COPZ function, leading to the impairment of its protein-binding ability. | ||||||
Withaferin A | 5119-48-2 | sc-200381 sc-200381A sc-200381B sc-200381C | 1 mg 10 mg 100 mg 1 g | $127.00 $572.00 $4090.00 $20104.00 | 20 | |
Withaferin A binds to annexin II, a protein that interacts with COPZ, leading to the inhibition of the complex formation between annexin II and COPZ, which is essential for COPZ's function in vesicular trafficking. | ||||||
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 inhibits the activity of N-WASP, a regulatory protein that controls actin polymerization. Since COPZ is involved in vesicle formation and transport, actin polymerization is critical for this process, inhibition of N-WASP by Wiskostatin can lead to the functional inhibition of COPZ by impairing vesicle movement. | ||||||
ML 141 | 71203-35-5 | sc-362768 sc-362768A | 5 mg 25 mg | $134.00 $502.00 | 7 | |
ML141 is a selective inhibitor of Cdc42, a small GTPase involved in cytoskeletal organization. COPZ function is closely related to cytoskeletal dynamics, and by inhibiting Cdc42, ML141 can impair the ability of COPZ to participate in vesicle trafficking processes. | ||||||
Dynamin Inhibitor I, Dynasore | 304448-55-3 | sc-202592 | 10 mg | $87.00 | 44 | |
Dynasore inhibits dynamin, a GTPase involved in the scission of clathrin-coated vesicles from the membrane. Since COPZ is part of the coat protein complex I (COPI) involved in vesicle formation, inhibiting dynamin function with Dynasore can inhibit COPZ function by disrupting vesicle scission, an essential step in vesicular transport. | ||||||
Chlorpromazine | 50-53-3 | sc-357313 sc-357313A | 5 g 25 g | $60.00 $108.00 | 21 | |
Chlorpromazine is known to disassemble clathrin lattices on vesicles. Since COPZ is associated with the COPI vesicle coat, destabilizing clathrin structures with Chlorpromazine can indirectly inhibit COPZ by interfering with vesicular trafficking pathways, which require the cooperative action of various coat proteins, including COPZ. | ||||||
Brefeldin A | 20350-15-6 | sc-200861C sc-200861 sc-200861A sc-200861B | 1 mg 5 mg 25 mg 100 mg | $30.00 $52.00 $122.00 $367.00 | 25 | |
Brefeldin A disrupts the Golgi apparatus by inhibiting ADP-ribosylation factor (ARF) proteins. Since COPZ is involved in the retrograde Golgi-to-ER transport, the inhibition of ARF proteins by Brefeldin A can lead to the inhibition of COPZ by disrupting the formation and maintenance of COPI vesicles, thereby impairing COPZ-mediated transport. | ||||||
Exo2 | 304684-77-3 | sc-215011 sc-215011A | 5 mg 25 mg | $87.00 $282.00 | 1 | |
Exo2 inhibits the assembly of the exocyst complex, which is involved in vesicle tethering to the plasma membrane. By inhibiting exocyst complex formation, Exo2 can indirectly inhibit COPZ by disrupting the overall vesicle transport and docking process, which is necessary for the proper function of COPZ in vesicular trafficking. | ||||||
SecinH3 | 853625-60-2 | sc-203260 | 5 mg | $273.00 | 6 | |
SecinH3 inhibits cytohesins, which are guanine nucleotide exchange factors for ARF GTPases. By inhibiting cytohesins, SecinH3 can lead to the functional inhibition of COPZ by reducing the activation of ARF GTPases, which are necessary for the formation of COPI vesicles where COPZ operates. | ||||||
Pitstop 2 | 1419320-73-2 | sc-507418 | 10 mg | $360.00 | ||
Pitstop 2 inhibits the interaction between clathrin terminal domain and clathrin-box motif-containing proteins. While COPZ is part of the COPI complex, it is functionally linked to clathrin-mediated processes, and Pitstop 2 can indirectly inhibit COPZ function by disrupting the formation of clathrin-coated vesicles, which can impact COPZ-mediated trafficking. | ||||||