Heterogeneous nuclear ribonucleoprotein D0 (AUF1) (HNRNPD)

Heterogeneous nuclear ribonucleoprotein D0, commonly known as AUF1, is a multifunctional RNA-binding protein that plays a pivotal role in the post-transcriptional regulation of gene expression. It specifically recognizes and binds to AU-rich elements (AREs) located in the 3' untranslated regions (UTRs) of many short-lived mRNAs, including those encoding cytokines, growth factors, and proto-oncogenes (UniProt Q14103). AUF1 exists as four distinct isoforms (p37, p40, p42, and p45) produced by alternative splicing, which cooperatively regulate mRNA stability and translation (PMID: 12514175). While its primary function is to promote mRNA decay by recruiting the exosome complex, it can also stabilize certain transcripts or facilitate their translation depending on the cellular environment and isoform composition (PMID: 23536156). In human diseases, AUF1 is frequently dysregulated; its overexpression is linked to various cancers where it may stabilize oncogenic mRNAs or degrade tumor suppressors, while its deficiency is associated with chronic inflammatory conditions due to the failure to degrade pro-inflammatory cytokine mRNAs like TNF-alpha (PMID: 15107404). Although no specific small-molecule inhibitors are currently approved for clinical use, AUF1 remains a significant target for therapeutic research in oncology and immunology, with experimental modulation achieved through natural products like resveratrol or nucleic acid-based therapies (PMID: 21602001).

Other names

AUF1AU-rich element RNA-binding protein 1hnRNP D0P37P40P42P45

AUF1 binds to AU-rich elements (AREs) in the 3' untranslated regions (UTRs) of target mRNAs and recruits the exosome complex and other decay factors to promote rapid mRNA degradation.