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Pre-mRNA processing factor 38A (PRPF38A) is an essential spliceosomal protein that plays a critical role during spliceosome activation and pre-mRNA splicing[1][3]. It enables RNA binding activity and is part of the U2-type precatalytic spliceosome, localized to the nucleoplasm[1][3]. Structurally, its amino-terminal domain is organized around three pairs of antiparallel α-helices, functioning primarily as a versatile protein–protein interaction hub[1]. PRPF38A coordinates the sequential exchange of partner proteins required for the precise folding and assembly of the U2/U6 catalytic RNA core—a prerequisite for forming a catalytically active spliceosome[1]. Knockdown of PRPF38A disrupts the splicing of a subset of genes, affecting alternative splicing events such as retained introns, and selectively alters transcripts essential for cell processes like mitosis, apoptosis, and immune response[2]. These functions highlight PRPF38A as a multifunctional regulator of transcriptome integrity and cellular viability, with particular relevance in cancer biology such as triple-negative breast cancer[2].
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