Phospholipid scramblase 1 (PLSCR1)

Phospholipid scramblase 1 (PLSCR1) is a multifunctional protein originally characterized for its ability to catalyze calcium-dependent, ATP-independent translocation (“scrambling”) of phospholipids across cell membranes. Beyond this, PLSCR1 is now recognized as an interferon-stimulated gene (ISG) with direct antiviral activity against a range of viruses (including SARS-CoV-2, influenza A, HIV, HBV, HCMV, and EBV), operating through both inhibition of viral entry/fusion and transcriptional regulation of immune response pathways[1][2][3]. PLSCR1 can enhance the transcription of ISGs and type III interferon receptors, modulate the JAK/STAT pathway, and help protect tissues from immunopathology during infection. Dysregulation or overexpression of PLSCR1 has been implicated in cancer cell proliferation, migration, and therapy resistance, particularly in basal-like breast cancer and primary liver cancer, suggesting context-dependent roles in disease[1][4]. No approved drugs directly target PLSCR1 yet, but it is considered a candidate therapeutic target for enhancing antiviral immunity and as a biomarker for interferon response modulation[1][2][3][4].

Other names

Phospholipid scramblase 1PLSCR1PL scramblase 1MMTRA1BCa(2+)-dependent phospholipid scramblase 1Erythrocyte phospholipid scramblaseMg(2+)-dependent nucleaseMmTRA1b

For potential future PLSCR1 agonists: enhancement of antiviral immunity by upregulation of type III interferon signaling, promotion of ISG expression, and membrane-mediated viral restriction[1][2][3].