Functional and
Network Analysis of PRPF3: Insights into Spliceosomal Regulation and Disease Associations
Farzia Kasala, Adiga Usha, Amulya Tunuguntla and Sampara Vasishta
Res. J. Biotech.; Vol. 20(12); 47-54;
doi: https://doi.org/10.25303/2012rjbt047054; (2025)
Abstract
Pre-mRNA Processing Factor 3 (PRPF3) is a key component of the spliceosomal complex,
involved in pre-mRNA splicing, ribonucleoprotein assembly and RNA stability. Mutations
in PRPF3 have been linked to retinitis pigmentosa, cancer and neurodegenerative
disorders, highlighting its clinical significance. This study aimed to analyze PRPF3’s
protein interaction network, functional pathways and disease associations to better
understand its biological role. A protein-protein interaction (PPI) network was
constructed using STRING, followed by functional enrichment analysis using Gene
Ontology (GO), KEGG and Reactome databases. Subcellular localization was assessed
using the COMPARTMENTS database, while pathway enrichment was validated using Benjamini-Hochberg
multiple testing correction.
PRPF3 exhibited strong interactions within the spliceosome (hsa03040, p = 6.66E-22),
particularly in U4/U6-U5 tri-snRNP assembly. GO enrichment analysis confirmed its
role in mRNA splicing (GO:0000398, p = 2.24E-17) and snRNA binding (GO:0017069,
p = 0.0041). PRPF3 localized predominantly to the spliceosomal complex, nuclear
speck and Cajal body. Notably, mRNA decay pathways (HSA-430039, p = 0.0146) suggest
a secondary role in RNA turnover. PRPF3 is a key spliceosomal protein, influencing
pre-mRNA processing and RNA metabolism. Its association with retinitis pigmentosa
and cancer suggests therapeutic potential in targeting PRPF3-related splicing defects.
Future studies should explore gene-editing interventions to correct PRPF3 mutations.
