KIF1C Activators
KIF1C Activators are a collection of chemical compounds that facilitate and enhance the functional activity of the motor protein KIF1C through various indirect mechanisms influencing cellular signaling and microtubule dynamics. Phosphatidylinositol 3-phosphate (PI3P) strengthens KIF1C's interaction with endosomes, thereby boosting its cargo transport capabilities, while Adenosine triphosphate (ATP) directly fuels KIF1C's motor function, as ATP hydrolysis is essential for its movement along microtubules. Paclitaxel's microtubule-stabilizing effects provide a more robust and stable track for KIF1C to convey vesicular cargo. Insulin and Epidermal Growth Factor (EGF) both activate pathways that culminate in the production of PI3P or stimulate vesicular dynamics, which can indirectly enhance the transport efficiency of KIF1C. Zoledronic acid's inhibition of farnesyl pyrophosphate synthase and the subsequent impact on small GTPase prenylation may necessitate an upregulation in vesicle trafficking, potentially increasing KIF1C activity to compensate for altered cellular transport mechanisms.
Further influencing KIF1C activity, Dibutyryl-cAMP and Forskolin both raise intracellular cAMP levels, thereby activating PKA, which may phosphorylate proteins within the vesicle trafficking pathway and consequently augment KIF1C's transport capacity. Okadaic acid, through the inhibition of protein phosphatases, could lead to a hyperphosphorylated state that favors KIF1C-mediated vesicle movement. Brefeldin A disrupts the Golgi apparatus, increasing the demand for retrograde vesicle transport, a process in which KIF1C could play a compensatory role. Lithium chloride's inhibition of GSK-3 potentially enhances KIF1C function by stabilizing microtubules, ensuring a more reliable pathway for KIF1C-mediated transport. Lastly, ML-9's inhibition of MLCK may shift the balance of cytoskeletal dynamics in favor of microtubule-based transport, reducing competition from actin filaments and indirectly enhancing the transport activity of KIF1C. Collectively, these activators work through distinct yet converging pathways to enhance the functional activity of KIF1C, promoting its role in intracellular cargo transport without direct activation or upregulation of expression.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
ATP | 56-65-5 | sc-507511 | 5 g | $17.00 | ||
ATP is the primary energy source for motor proteins, including KIF1C. Hydrolysis of ATP to ADP provides the necessary energy for the conformational changes that drive KIF1C movement along microtubules. Higher concentrations of ATP would thus enhance KIF1C's motor activity. | ||||||
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, preventing their depolymerization. By stabilizing microtubules, paclitaxel can enhance the ability of KIF1C to transport cargo along these structures, as KIF1C is less likely to encounter destabilized microtubules that can hinder its motor function. | ||||||
Insulin | 11061-68-0 | sc-29062 sc-29062A sc-29062B | 100 mg 1 g 10 g | $156.00 $1248.00 $12508.00 | 82 | |
Insulin signaling can lead to the activation of PI3K and the production of PI3P, which, as mentioned above, can enhance KIF1C’s endosome binding and transport function. | ||||||
Zoledronic acid, anhydrous | 118072-93-8 | sc-364663 sc-364663A | 25 mg 100 mg | $92.00 $256.00 | 5 | |
Zoledronic acid inhibits farnesyl pyrophosphate synthase, which can alter the prenylation and function of small GTPases involved in vesicle trafficking. This could lead to increased vesicle transport requirements and thus potentially increase the activity of KIF1C in the cell as it compensates for the alterations. | ||||||
Dibutyryl-cAMP | 16980-89-5 | sc-201567 sc-201567A sc-201567B sc-201567C | 20 mg 100 mg 500 mg 10 g | $47.00 $136.00 $492.00 $4552.00 | 74 | |
Dibutyryl-cAMP, a cAMP analog, activates PKA which can phosphorylate various proteins involved in vesicle trafficking. The phosphorylation of these substrates may enhance KIF1C-mediated transport of vesicles by altering their interaction with the motor protein or modifying the motor protein itself. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $291.00 $530.00 $1800.00 | 78 | |
Okadaic acid is a potent inhibitor of protein phosphatases PP1 and PP2A, leading to increased phosphorylation levels of cellular proteins. Hyperphosphorylation can modulate vesicle transport and motor protein interactions, potentially enhancing KIF1C-mediated cargo transport. | ||||||
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 disrupts the Golgi apparatus and enhances retrograde transport to the endoplasmic reticulum, which may indirectly enhance the activity of KIF1C as it is involved in the transport of vesicles and could be recruited to compensate for disrupted cellular transport mechanisms. | ||||||
Forskolin | 66575-29-9 | sc-3562 sc-3562A sc-3562B sc-3562C sc-3562D | 5 mg 50 mg 1 g 2 g 5 g | $78.00 $153.00 $740.00 $1413.00 $2091.00 | 73 | |
Forskolin activates adenylate cyclase, increasing intracellular cAMP levels and subsequently activating PKA. PKA can phosphorylate proteins involved in vesicle trafficking, potentially enhancing KIF1C's role in the transport of vesicles by modifying the interaction dynamics between KIF1C and its cargoes. | ||||||
Lithium | 7439-93-2 | sc-252954 | 50 g | $214.00 | ||
Lithium chloride inhibits GSK-3, which can lead to alterations in microtubule dynamics and potentially enhance the activity of microtubule-associated motor proteins such as KIF1C by stabilizing the tracks along which KIF1C moves. | ||||||
ML-9 | 105637-50-1 | sc-200519 sc-200519A sc-200519B sc-200519C | 10 mg 50 mg 100 mg 250 mg | $112.00 $449.00 $673.00 $1224.00 | 2 | |
ML-9 is an inhibitor of myosin light chain kinase (MLCK) and can affect cytoskeletal dynamics. By altering actin filament organization, ML-9 could indirectly enhance microtubule-based transport and thus KIF1C's activity by reducing competition between actin and microtubule-based transport systems. | ||||||