PLRG1 Inhibitors
Chemical inhibitors of PLRG1 employ various strategies to impede its functional role within the spliceosome, the molecular complex responsible for splicing pre-mRNA. Staurosporine targets the kinases that regulate PLRG1 through phosphorylation, a post-translational modification essential for PLRG1's activity in spliceosome assembly and function. By inhibiting these kinases, Staurosporine effectively reduces PLRG1's ability to contribute to the RNA splicing process. Similarly, U0126 disrupts the MAPK/ERK pathway by inhibiting MEK, which subsequently reduces the signaling required for the proper assembly of spliceosomal components involving PLRG1, thereby diminishing its role in RNA splicing. LY294002's inhibition of PI3K attenuates the phosphorylation status of various proteins, potentially including those that interact with or regulate PLRG1, leading to an indirect inhibition of PLRG1's spliceosome-related functions. Alsterpaullone, through its inhibition of cyclin-dependent kinases, can prevent the cell cycle-related events that are necessary for the proper function of PLRG1 in the spliceosome.
Further, the chemical inhibitor 5-Fluorouracil interferes with RNA processing, a pathway central to PLRG1's operational domain; this disruption leads to an indirect inhibition of PLRG1's role in this process. Trichostatin A, an HDAC inhibitor, can alter chromatin structure and affect the transcription of spliceosome components, potentially leading to a compromised spliceosomal assembly where PLRG1 is active. Geldanamycin binds to Hsp90, destabilizing its interaction with PLRG1, which may result in a dysfunctional spliceosome and, subsequently, inhibited PLRG1 function. Pladienolide B targets the SF3b complex within the spliceosome, and its binding can lead to aberrant splicing, which indirectly hampers PLRG1's performance. Additionally, Silvestrol impedes the initiation factor eIF4A, which can have downstream effects on the synthesis of proteins essential for PLRG1's activity in splicing. Bortezomib, a proteasome inhibitor, creates a backlog of misfolded proteins, inducing cellular stress that could hinder the assembly of the spliceosome and thus inhibit PLRG1 indirectly. Lastly, Indisulam promotes the degradation of RBM39, a constituent of the spliceosome, potentially disrupting the splicing process that PLRG1 is part of, leading to its functional inhibition.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Staurosporine | 62996-74-1 | sc-3510 sc-3510A sc-3510B | 100 µg 1 mg 5 mg | $82.00 $150.00 $388.00 | 113 | |
Staurosporine is a potent kinase inhibitor that can inhibit PLRG1 by targeting the kinases involved in its regulatory phosphorylation, thereby preventing PLRG1's functional activity in the spliceosome complex. | ||||||
U-0126 | 109511-58-2 | sc-222395 sc-222395A | 1 mg 5 mg | $63.00 $241.00 | 136 | |
U0126 is an inhibitor of MEK, which is part of the MAPK/ERK pathway. By inhibiting MEK, the downstream signaling that may regulate the assembly or activity of spliceosomal complexes involving PLRG1 is inhibited, therefore indirectly inhibiting PLRG1's function in RNA splicing. | ||||||
LY 294002 | 154447-36-6 | sc-201426 sc-201426A | 5 mg 25 mg | $121.00 $392.00 | 148 | |
LY294002 inhibits PI3K, a kinase upstream of many signaling pathways, including those that control the assembly of spliceosomal components. Inhibition of PI3K can lead to reduced phosphorylation status of proteins that interact with or regulate PLRG1, thus inhibiting PLRG1's function in the spliceosome. | ||||||
Fluorouracil | 51-21-8 | sc-29060 sc-29060A | 1 g 5 g | $36.00 $149.00 | 11 | |
5-Fluorouracil can inhibit RNA processing and maturation which are processes that PLRG1 is involved in. Although not a direct inhibitor, by disrupting the general RNA maturation machinery, it indirectly inhibits the functional role of PLRG1 in these processes. | ||||||
Trichostatin A | 58880-19-6 | sc-3511 sc-3511A sc-3511B sc-3511C sc-3511D | 1 mg 5 mg 10 mg 25 mg 50 mg | $149.00 $470.00 $620.00 $1199.00 $2090.00 | 33 | |
Trichostatin A is a histone deacetylase (HDAC) inhibitor that can alter chromatin structure and affect the transcription of certain spliceosome components, which might indirectly inhibit PLRG1 by disrupting the proper assembly of the spliceosome where PLRG1 functions. | ||||||
Alsterpaullone | 237430-03-4 | sc-202453 sc-202453A | 1 mg 5 mg | $67.00 $306.00 | 2 | |
Alsterpaullone is a cyclin-dependent kinase (CDK) inhibitor, which can inhibit the cell cycle and subsequently the phosphorylation of proteins involved in splicing, indirectly inhibiting the spliceosomal function of PLRG1. | ||||||
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $38.00 $58.00 $102.00 $202.00 | 8 | |
Geldanamycin binds to Hsp90, a chaperone involved in the proper folding and function of many proteins, including those within spliceosomal complexes. Inhibition of Hsp90 can prevent proper PLRG1 function by destabilizing spliceosome assembly or activity. | ||||||
Pladienolide B | 445493-23-2 | sc-391691 sc-391691B sc-391691A sc-391691C sc-391691D sc-391691E | 0.5 mg 10 mg 20 mg 50 mg 100 mg 5 mg | $290.00 $5572.00 $10815.00 $25000.00 $65000.00 $2781.00 | 63 | |
Pladienolide B binds to the SF3b complex of the spliceosome, disrupting its function. As PLRG1 is associated with the spliceosome, the disruption of SF3b by Pladienolide B would indirectly inhibit the function of PLRG1 by destabilizing the spliceosome complex it operates within. | ||||||
Silvestrol | 697235-38-4 | sc-507504 | 1 mg | $920.00 | ||
Silvestrol, an inhibitor of the eukaryotic initiation factor 4A (eIF4A), can indirectly inhibit PLRG1's function by inhibiting translation initiation, which may affect the synthesis of proteins that are essential for PLRG1's role in splicing. | ||||||
Bortezomib | 179324-69-7 | sc-217785 sc-217785A | 2.5 mg 25 mg | $132.00 $1064.00 | 115 | |
Bortezomib is a proteasome inhibitor that can lead to the accumulation of misfolded proteins, causing cellular stress and potentially affecting the assembly of the spliceosome, thus indirectly inhibiting the function of PLRG1 within this complex. | ||||||