PRRC2C (proline-rich coiled-coil 2C) is a multifunctional protein with roles in mRNA processing and stress response. Structurally, PRRC2C localizes to the cytosol and contains RNA-binding domains 1. Its primary function involves stress granule formation; PRRC2C is identified as a core component critical for assembly of microscopically visible stress granules under cellular stress 1. Mechanistically, PRRC2C promotes leaky scanning during translation initiation by binding eukaryotic translation initiation factors and enriching on ribosomes translating mRNAs with upstream open reading frames (uORFs), thereby regulating translation of uORF-containing transcripts 2. In disease contexts, PRRC2C shows significant clinical relevance. In hepatocellular carcinoma, elevated PRRC2C expression correlates with shorter overall survival and promotes cancer cell proliferation, migration, and invasion through epithelial-mesenchymal transition pathways 3. PRRC2C mutations are enriched in responders to atezolizumab immunotherapy in non-small cell lung cancer 4, and alternative splicing of PRRC2C is dysregulated in lung cancer 5. Additionally, PRRC2C is identified as a potential biomarker in preeclampsia pathophysiology 6, and functions as a lncRNA regulating vascular calcification through the miR-145-5p/Smad3 axis 7. These diverse roles suggest PRRC2C participates in both normal mRNA metabolism and cancer-associated pathways.