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Last update 08 May 2025

PRPF8

Last update 08 May 2025

Basic Info

Synonyms

220 kDa U5 snRNP-specific protein, hPrp8, p220

+ [9]

Introduction

Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes, both of the predominant U2-type spliceosome and the minor U12-type spliceosome (PubMed:10411133, PubMed:11971955, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30315277, PubMed:30705154, PubMed:30728453). Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex, a building block of the spliceosome. Functions as a scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site.

Drugs associated with PRPF8

CN117222660

Patent Mining

Target

PRPF8

Mechanism-

Active Org.

Flux Therapeutics, Inc.

Originator Org.

Flux Therapeutics, Inc.

Active Indication

Congenital Disorders [+3]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with PRPF8

100 Translational Medicine associated with PRPF8

0 Patents (Medical) associated with PRPF8

394

Literatures (Medical) associated with PRPF8

03 May 2025·Journal of Biomolecular Structure and Dynamics

Molecular docking and MD simulations reveal protease inhibitors block the catalytic residues in Prp8 intein of Aspergillus fumigatus: a potential target for antimycotics

Article

Author: Panda, Sunita ; Pati, Sanghamitra ; Rout, Madhusmita ; Dehury, Budheswar ; Turuk, Jyotirmayee ; Mishra, Sarbani

Resistance to azoles and amphotericin B especially in Aspergillus fumigatus is a growing concern towards the treatment of invasive fungal infection. At this critical juncture, intein splicing would be a productive, and innovative target to establish therapies against resistant strains. Intein splicing is the central event for the activation of host protein, essential for the growth and survival of various microorganisms including A. fumigatus. The splicing process is a four-step protease-like nucleophilic cascade. Thus, we hypothesise that protease inhibitors would successfully halt intein splicing and potentially restrict the growth of the aforementioned pathogen. Using Rosetta Fold and molecular dynamics simulations, we modelled Prp8 intein structure; resembling classic intein fold with horse shoe shaped splicing domain. To fully comprehend the active site of Afu Prp8 intein, C1, T62, H65, H818, N819 from intein sequences and S820, the first C-extein residue are selected. Molecular docking shows that two FDA-approved drugs, i.e. Lufotrelvir and Remdesivir triphosphate efficiently interact with Prp8 intein from the assortment of 212 protease inhibitors. MD simulation portrayed that Prp8 undergoes conformational change upon ligand binding, and inferred the molecular recognition and stability of the docked complexes. Per-residue decomposition analysis confirms the importance of F: block R802, V803, and Q807 binding pocket in intein splicing domain towards recognition of inhibitors, along with active site residues through strong hydrogen bonds and hydrophobic contacts. However, in vitro and in vivo assays are required to confirm the inhibitory action on Prp8 intein splicing; which may pave the way for the development of new antifungals for A. fumigatus.

01 Apr 2025·Stem Cell Research

Generation of a human iPSC line with heterozygous PRPF8 c.5792C > T, p. T1931M mutation to model retinitis pigmentosa using CRISPR/Cas9 technology

Article

Author: Liang, Yuqin ; Cui, Zekai ; Gu, Jianing ; Liang, Yuan ; Chen, Yuexi ; Chen, Jiansu ; Duan, Chunwen ; Li, Xiaoxue ; Sun, Xihao ; Ding, Chengcheng ; Chen, Hang

Mutations in the PRPF8 gene frequently result in retinitis pigmentosa (RP), an autosomal dominant inherited retinal disease that can lead to nyctalopia and progressive vision loss. Currently, no effective treatment is available. In this study, we used CRISPR/Cas9 technology to introduce a heterozygous point mutation inthe PRPF8 gene of a normal induced pluripotent stem cell (iPSC) line. This mutation mirrors that found in a previously reportedRP patient-derived iPSC line (CSUASOi006-A) from our group. Establishing the PRPF8 gene mutation cell line (CSUASOi012-A-2) provides a valuable cellular resource for studying the pathogenesis of RP.

01 Apr 2025·Free Radical Biology and Medicine

Excision Repair Cross Complementation Group 1 gene exon 3 skipping isoform presents selective cGAS-STING activation in Platinum-sensitive lung adenocarcinoma

Article

Author: Zhang, Liang ; Wu, Shengwen ; Xiao, Mingyang ; Jin, Cuihong ; Zhao, Shuang ; Lu, Xiaobo ; Li, Liuli ; Zhang, Guopei ; Yang, Jinghua

Platinum-based chemotherapy is widely used as a frontline therapy for lung adenocarcinoma, while its efficacy is limited by agent resistance and severe toxicity. Recently the immunotherapy represents an alternative or complement to Platinum-based chemotherapy. Interestingly, the sensitivity to platinum is known as a relevant phenotypical biomarker of valid immunotherapy due to the defects in DNA damage response (DDR) in cancer cells. The cGAS/STING pathway detects cytosolic DNA to activate innate immune response, which seems to become a bridge linking DDR and cancer immunogenicity. This study aimed to investigate the effect of ERCC1 splicing isoforms on the cGAS/STING pathway. Besides, the association of ERCC1 splicing isoforms with cGAS/STING signaling in cisplatin-treated cells was analyzed, and the modulation of PRPF8 on ERCC1 exon skipping splicing was elucidated by RNA immunoprecipitation. Finally, we also explored the potential role of an herbal extract β-elemene as chemosensitizer and activator of cGAS/STING signaling. We demonstrated that ERCC1 exon 3 inclusion was of equal importance to exon 8 and endowed ERCC1 with an elevated DNA repair activity, which was linked with cisplatin resistance and cGAS-STING suppression. Mechanistically, PRPF8 was identified to be directly interacted with modulating ERCC1 exon 3 skipping, while β-elemene was found to be involved in the activation of cGAS-STING signaling as an inhibitor of PRPF8. Our data reveal that the ERCC1 exon 3 skipping isoform is associated with DDR and the cGAS/STING innate immune pathway, which provide preclinical rationale for using alternative or complement immunotherapy in Platinum-sensitive NSCLC patients.

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PRPF8

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