hnRNP D

Heterogeneous nuclear ribonucleoprotein D (hnRNP D), also known as AUF1, is a multifunctional RNA-binding protein that regulates RNA metabolism, including mRNA stability and alternative splicing^[1][2]. Mechanistically, hnRNP D contains two DNA/RNA-binding domains that specifically interact with single-stranded telomeric DNA repeats, allowing it to unfold quadruplex structures and influence telomere elongation by telomerase^[1]. This activity distinguishes hnRNP D from related isoforms, as the base-specific binding of its BD2 domain enables selective recognition of the d(TAG) segment^[1]. In disease models, hnRNP D has been implicated in the maintenance of genomic stability, potentially affecting cellular senescence and cancer-associated telomere dynamics^[1][2]. Compared with other hnRNP family members, hnRNP D uniquely couples nucleic acid binding with structural remodeling of DNA/RNA secondary structures, highlighting its specialized role among AUF1 isoforms^[1]. For experimental applications, hnRNP D’s interaction with single-stranded DNA and RNA has been exploited in vitro to study telomere processing and mRNA degradation, providing a platform for investigating post-transcriptional regulation mechanisms^[1][2]. Collectively, hnRNP D serves as a critical regulator of nucleic acid architecture, with functional distinctions that support targeted research on RNA stability, telomere maintenance, and associated disease processes^[1][2].