Zinc finger RNA-binding protein (ZFR)

Zinc finger RNA-binding protein (ZFR) is a conserved RNA-binding protein characterized by three N-terminal C2H2 zinc finger motifs and a C-terminal DZF (domain associated with zinc fingers) domain, the latter having a nucleotidyltransferase fold but lacking enzymatic activity[2][4]. ZFR engages in post-transcriptional RNA processing, alternative splicing, and nucleocytoplasmic shuttling of target RNAs (such as Staufen homolog 2 in neurons)[4][5]. It acts as a repressor of the interferon response via alternative splicing regulation, coordinates crosstalk between RNA decay and transcription, and may heterodimerize with other DZF domain-containing RNA-binding proteins (e.g., ILF2/NF45, ILF3/NF90)[2]. ZFR is crucial in developmental stages (specifically postimplantation and gastrulation)[5], regulates innate immune responses in macrophages, and is implicated in pancreatic cancer where its elevated expression promotes cell viability and invasion[4]. The gene has also been linked to hereditary spastic paraplegia (SPG71) in humans. No therapeutic drugs directly targeting ZFR are currently documented. It is considered a valid biomedical target due to its role in central RNA regulatory and immune pathways, and its biomarker potential in oncology[4]. Targeting ZFR for therapy is challenged by its fundamental roles in RNA metabolism and immune modulation, posing the risk of systemic effects and developmental toxicity[5].

Other names

ZFRhZFRZFR1SPG71M-phase phosphoprotein homologZinc finger RNA-binding protein