rbp

RBP stands for RNA-binding protein, a broad and diverse class of proteins that interact with RNA molecules to influence post-transcriptional gene regulation. RBPs commonly bind to messenger RNA or noncoding RNAs through sequence or structure motifs, or a combination thereof, and function within ribonucleoprotein complexes to control RNA processing, transport, localization, translation, and decay. They are found across all domains of life and are essential for development and cellular homeostasis.

Many RBPs contain conserved RNA-binding domains, such as the RNA recognition motif (RRM), KH domains, zinc finger modules, or Pumilio repeats, which determine their RNA targets and binding modes. Some recognize short linear motifs, others bind structured elements in the RNA. RBPs can act cooperatively or competitively and may shuttle between nucleus and cytoplasm to coordinate RNA life cycle steps.

The functions of RBPs are diverse. They participate in splicing and polyadenylation in the nucleus, regulate mRNA export, determine subcellular localization, modulate translation efficiency, and influence mRNA stability and decay. They also participate in processing of noncoding RNAs and in the assembly of ribonucleoprotein particles, including processing bodies and stress granules.

Dysregulation or mutation of RBPs is linked to human disease, including cancer, neurodegenerative disorders such as ALS and fragile X syndrome, and developmental abnormalities. Well-known examples include ELAVL1/HuR, which stabilizes AU-rich element-containing mRNAs; TDP-43, implicated in neurodegeneration; and FMRP, which modulates neuronal mRNA transport and translation.

RBPs are studied using techniques such as RNA immunoprecipitation (RIP) and crosslinking and immunoprecipitation (CLIP) methods (eCLIP, iCLIP, PAR-CLIP) to map RNA-binding sites and targets genome-wide.