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Nuclear RNA export factor 1 (NXF1), also known as TAP, is a protein encoded by the NXF1 gene in humans[5]. It is a central component of the mRNA nuclear export pathway, shuttling between the nucleus and cytoplasm to mediate the export of processed mRNA transcripts through the nuclear pore complex[1][3][4][5]. Structurally, NXF1 contains several domains—including an RNA recognition motif (RRM), leucine-rich repeats (LRRs), a nuclear transport factor 2-like (NTF2L) domain that enables heterodimerization with NXT1, and a ubiquitin-associated (UBA) domain enabling interaction with nucleoporins[3][5]. NXF1 is functionally conserved from yeast (Mex67) to humans and is essential for gene expression by ensuring that only properly processed mRNAs are exported to the cytoplasm for translation[1][3][4]. NXF1 interacts with specific adaptor proteins to achieve this selectivity, and its recruitment is coupled to RNA splicing and processing events[1]. Although not a common direct therapeutic target, its fundamental role in gene expression makes it vital to cell viability, and disruption can have broad detrimental effects[1][5]. There is no current evidence for clinically targeted drugs or its use as a biomarker.
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