{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPhospholipid scramblase 1 (PLSCR1) is a multifunctional, Ca²⁺‐binding, and multiply palmitoylated endofacial plasma membrane protein that mediates the rapid, energy‐independent transbilayer redistribution of phospholipids—most notably the externalization of phosphatidylserine—in response to increased intracellular Ca²⁺. This scrambling activity plays a key role in processes such as apoptotic cell clearance, blood coagulation, and membrane remodeling in activated platelets and other cell types. Furthermore, PLSCR1 is enriched in lipid raft microdomains, where its regulated palmitoylation governs its trafficking between the plasma membrane and the nucleus."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in lipid scrambling, PLSCR1 acts as a versatile signal modulator. It is inducible by interferons and growth factors and functions as a substrate for intracellular kinases such as Src, Abl, and PKCδ. In several hematopoietic and leukemic models, PLSCR1 contributes to cytokine‐regulated cell proliferation, differentiation, and myelopoiesis. Its dynamic nuclear trafficking—mediated by a noncanonical nuclear localization signal and importin α/β—allows it to bind genomic DNA and modulate gene expression (for example, enhancing the transcription of the inositol 1,4,5-triphosphate receptor type 1). These interconnected plasma membrane and nuclear functions underline its role in cell differentiation and response to cytokine as well as growth factor signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPLSCR1 additionally participates in host antiviral defenses and virus–host interactions. It interacts directly with key viral regulatory proteins—including HIV-1 Tat, hepatitis B virus (HBV) X protein, hepatitis C virus (HCV) envelope glycoproteins, Epstein–Barr virus (EBV) transactivators, and HTLV-1 Tax—and its antiviral action has been demonstrated against a range of RNA and DNA viruses. In the context of emerging pathogens, recent evidence indicates that PLSCR1 functions as a potent cell-autonomous restriction factor against SARS-CoV-2 by targeting virus-containing vesicles and preventing spike-mediated fusion, thereby blocking viral entry via both endocytic and cell surface fusion pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to these roles, PLSCR1 interacts with a variety of cellular proteins—including proteinase 3, extracellular matrix components (such as ECM1), BACE, and receptors like CD4 and RELT—to influence intracellular trafficking, receptor recycling, and the regulation of autophagy and apoptosis. Its expression is deregulated in several cancers and is associated with altered cell differentiation, tumor suppression, and progression, as seen in leukemias, breast cancer, ovarian cancer, and mantle cell lymphoma. Moreover, PLSCR1 has been implicated in neuronal apoptosis via interactions with Ca²⁺ channels (e.g. TRPC5), in environmental responsiveness such as heavy metal-induced activation and ozone-related epigenetic changes, and even in transcriptional regulation through factors like Snail. Together, these findings illustrate that PLSCR1 integrates membrane lipid remodeling with diverse signaling cascades and nuclear events, making it a central mediator of cellular responses in both physiological and pathological contexts."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}, {"type": "fg_f", "ref": "6"}, {"type": "fg_fs", "start_ref": "24", "end_ref": "42"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Quansheng Zhou, Ji Zhao, Therese Wiedmer, et al. 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