TTLL2 Inhibitors
Chemical inhibitors of tubulin tyrosine ligase-like 2 (TTLL2) can interfere with its function through various mechanisms, primarily by altering the phosphorylation state of proteins, inhibiting protein synthesis, or by directly affecting the substrate that TTLL2 modifies. Okadaic Acid and Calyculin A, both inhibitors of protein phosphatases PP1 and PP2A, can lead to an increase in the phosphorylation levels of a wide range of proteins, which includes those involved in the regulation of TTLL2. This hyperphosphorylated environment can hinder the activity of TTLL2 by modifying the proteins that are crucial for TTLL2's function in tubulin glutamylation. Similarly, Forskolin, by activating adenylyl cyclase, increases intracellular cAMP and consequently activates protein kinase A (PKA). Active PKA can phosphorylate proteins associated with TTLL2, affecting its activity. Conversely, H-89 acts to inhibit PKA, potentially reducing the phosphorylation of TTLL2 or its related proteins, thereby inhibiting TTLL2's function.
The other set of chemicals affects TTLL2 by targeting tubulin, its substrate. Colchicine, Vinblastine, Nocodazole, Podophyllotoxin, and Vincristine disrupt microtubule dynamics through various mechanisms such as inhibiting tubulin polymerization or promoting microtubule depolymerization. Such disruptions deprive TTLL2 of its substrate, inhibiting its ability to perform its enzymatic function of tubulin glutamylation. In contrast, Paclitaxel and Eribulin inhibit TTLL2 in a different manner; Paclitaxel stabilizes microtubules in such a way that they cannot undergo the structural changes necessary for TTLL2 to access and modify tubulin. Eribulin halts microtubule growth, thus preventing the formation of new microtubule structures needed for TTLL2 function. Lastly, Cycloheximide interferes with eukaryotic protein synthesis, which can result in a general decrease in the levels of TTLL2, as well as other proteins, thereby reducing TTLL2 activity indirectly. Each of these chemicals manipulates the cellular environment or the microtubule structures in such a way that TTLL2's ability to glutamylate tubulin is inhibited.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
Okadaic Acid, a marine toxin, functions as a potent inhibitor of protein phosphatases PP1 and PP2A. Inhibition of these phosphatases can increase the phosphorylation state of many proteins, potentially including TTLL2. Since TTLL2 is involved in tubulin glutamylation, a process regulated by phosphorylation, Okadaic Acid can inhibit TTLL2 through hyperphosphorylation, preventing its proper function in the modification of tubulin. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A sc-24000B sc-24000C | 10 µg 100 µg 500 µg 1 mg | $160.00 $750.00 $1400.00 $3000.00 | 59 | |
Calyculin A, another inhibitor of protein phosphatases PP1 and PP2A, operates in a similar manner to Okadaic Acid. By preventing the dephosphorylation of proteins, Calyculin A can lead to an aberrant phosphorylation state. TTLL2, due to its role in tubulin dynamics, may be negatively impacted by this increased phosphorylation, resulting in its functional inhibition. | ||||||
Forskolin | 66575-29-9 | sc-3562 sc-3562A sc-3562B sc-3562C sc-3562D | 5 mg 50 mg 1 g 2 g 5 g | $76.00 $150.00 $725.00 $1385.00 $2050.00 | 73 | |
Forskolin is an adenylyl cyclase activator, leading to an increase in intracellular cAMP levels. Elevated cAMP activates PKA, which can phosphorylate a wide range of targets, possibly including proteins associated with TTLL2. By altering the phosphorylation state, Forskolin can inhibit TTLL2 by changing the phosphorylation state of proteins that regulate TTLL2's tubulin glutamylation activity. | ||||||
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. TTLL2 is implicated in the post-translational modification of tubulin. By binding to tubulin, Colchicine can prevent the formation of microtubules, indirectly inhibiting TTLL2 by depriving it of its substrate, leading to a functional inhibition of its enzymatic activity. | ||||||
Vinblastine | 865-21-4 | sc-491749 sc-491749A sc-491749B sc-491749C sc-491749D | 10 mg 50 mg 100 mg 500 mg 1 g | $100.00 $230.00 $450.00 $1715.00 $2900.00 | 4 | |
Vinblastine disrupts microtubule assembly by binding to tubulin. This inhibition of microtubule formation can impede the ability of TTLL2 to modify tubulin, since TTLL2 enzymatic activity is dependent on the presence of polymerized microtubules. Therefore, Vinblastine functionally inhibits TTLL2 by obstructing its access to the substrate. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $58.00 $83.00 $140.00 $242.00 | 38 | |
Nocodazole interferes with microtubule polymerization. TTLL2, which modifies microtubule-based structures, would be functionally inhibited by Nocodazole, as the drug's action on microtubules would prevent TTLL2 from accessing its tubulin substrates to perform its glutamylation function. | ||||||
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 | $40.00 $73.00 $217.00 $242.00 $724.00 $1196.00 | 39 | |
Paclitaxel stabilizes microtubules and prevents their disassembly. By locking microtubules in a stable state, Paclitaxel may indirectly inhibit TTLL2 by preventing the dynamic structural changes of microtubules necessary for TTLL2 to access and modify its tubulin substrates. | ||||||
Eribulin | 253128-41-5 | sc-507547 | 5 mg | $865.00 | ||
Eribulin binds to the plus ends of microtubules, inhibiting their growth. By halting microtubule elongation, Eribulin would inhibit TTLL2 function by blocking the formation of new microtubular structures that TTLL2 needs to modify. | ||||||
Podophyllotoxin | 518-28-5 | sc-204853 | 100 mg | $82.00 | 1 | |
Podophyllotoxin binds to tubulin and inhibits its assembly into microtubules. This action would functionally inhibit TTLL2 by reducing the availability of polymerized microtubules, thus preventing TTLL2 from performing its enzyme-mediated glutamylation of tubulin. | ||||||
Cycloheximide | 66-81-9 | sc-3508B sc-3508 sc-3508A | 100 mg 1 g 5 g | $40.00 $82.00 $256.00 | 127 | |
Cycloheximide inhibits eukaryotic protein synthesis by interferingIt appears that there was a content loss in your previous message. You were likely referring to various chemical compounds and their potential effects on TTLL2, an enzyme involved in the post-translational modification of tubulin through glutamylation. | ||||||