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Nuclear assembly factor 1 ribonucleoprotein (NAF1) is an RNA-binding protein required for the maturation of box H/ACA small nucleolar ribonucleoproteins (snoRNPs) and plays a critical role in ribosome biogenesis and telomerase RNA stabilization. NAF1 associates with the H/ACA snoRNP complex during its assembly and is later replaced by GAR1 in mature complexes. It controls the stabilization of H/ACA RNAs, which include over 100 members such as snoRNAs and the telomerase RNA component, making it essential for proper ribosomal RNA modification and telomere length maintenance[3][4][5]. Loss-of-function mutations in NAF1 are linked to human hereditary syndromes involving pulmonary fibrosis, bone marrow failure, and telomere-related disorders, as well as increased susceptibility to myelodysplastic syndrome and liver disease[3][4]. Elevated NAF1 expression has been implicated in malignant phenotypes in cancers such as glioma, in part by promoting ribosome assembly and protein synthesis, and its transcription is regulated by oncogenes including c-Myc and NRF2[1]. NAF1 is considered essential for viability due to its roles in RNA maturation, but is not conventionally targeted by known therapeutic drugs, nor does it possess a classic receptor, enzyme, or ion channel function[4][5].
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