Proline-rich protein 13 (PRR13)

Proline-rich protein 13 (PRR13) is a small protein (~18.8 kDa, 187 amino acids) characterized by a high proportion of proline residues and a unique C-terminal serine sequence. PRR13 lacks well-characterized functional domains but is predominantly localized in the nucleus and is thought to act as a transcriptional regulator. It was initially discovered as a gene that mediates resistance to taxane chemotherapy (thus also called taxane-resistance protein 1, TXR1). PRR13 exerts its resistance effect by suppressing the transcription of thrombospondin-1 (TSP1), thereby preventing pro-apoptotic signaling and favoring tumor survival during chemotherapeutic treatment; silencing PRR13 increases cancer cell susceptibility to taxanes. Beyond chemoresistance, PRR13 expression is associated with cellular processes related to tumor progression, including cell adhesion, migration, angiogenesis, DNA repair, and immune microenvironment modulation. High expression of PRR13 correlates with poor prognosis in several cancers and may promote an immunosuppressive tumor microenvironment. Although highly expressed in tumor contexts, PRR13 does not appear essential for effector/memory T cell responses in at least some immune scenarios.

Other names

PRR13TXR1Taxane-resistance proteinBM-041FLJ23818DKFZP564J157proline-rich protein 13taxane-resistance protein

PRR13 suppresses the transcription of thrombospondin-1 (TSP1), reducing pro-apoptotic and anti-angiogenic effects, resulting in chemoresistance to taxane drugs. Silencing PRR13 (or TXR1) increases taxane sensitivity by elevating TSP1 and promoting apoptosis