Dicer–TAR RNA-binding protein complex (Dicer–TRBP complex) (Dicer–TRBP)

The Dicer–TAR RNA-binding protein complex (Dicer–TRBP complex) is a multi-protein assembly central to the RNA interference (RNAi) pathway, primarily responsible for the maturation of microRNAs (miRNAs) and small interfering RNAs (siRNAs). This complex is composed of the Dicer enzyme (DICER1), which contains two catalytic RNAse III domains, and the TAR RNA-binding protein (TRBP or TARBP2), which stabilizes Dicer and facilitates the efficient processing of precursor RNAs (UniProt Q9UPY3, Q15633). By converting precursor miRNAs (pre-miRNAs) into mature functional molecules, the complex regulates the post-transcriptional silencing of thousands of messenger RNAs (mRNAs) involved in development, cell proliferation, and apoptosis (PubMed 15973355). In various human cancers, the Dicer–TRBP complex is often dysregulated or mutated, leading to a global reduction in miRNA levels that can drive tumor progression and metastasis (PubMed 24508333). Additionally, the complex plays a role in viral infections, such as HIV-1, where it can be targeted or hijacked to influence viral replication. Therapeutic interest in this complex involves small molecules like enoxacin, which acts as a Dicer activator to restore miRNA biogenesis in cancer cells (PubMed 18347094). However, pharmacological modulation of this complex carries significant safety risks, as non-specific interference with the RNAi machinery can lead to widespread gene dysregulation and systemic toxicity.

Other names

DICER1–TARBP2 complexDicer–TRBP holoenzymeRISC-loading complex component

Enhancement of Dicer-mediated processing of precursor microRNAs (pre-miRNAs) into mature microRNAs (miRNAs) (PubMed 18347094); stabilization of the Dicer-TRBP interaction to improve catalytic efficiency.