{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nP‐selectin glycoprotein ligand‐1 (SELPLG), also known as PSGL‐1, is central to the initial tethering and rolling of leukocytes on activated vascular endothelium. Under mechanical stress, its binding to selectins exhibits a dual catch–slip bond behavior that prolongs bond lifetimes under low forces yet dissipates them when forces exceed a particular threshold—thereby providing a finely tuned mechanism for leukocyte adhesion and subsequent integrin activation. Critical post‐translational modifications (such as tyrosine sulfation and specific O‐glycosylation of its N‐terminal domain) determine its binding affinity and ligand specificity during these dynamic interactions."}, {"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 adhesion per se, SELPLG plays a pivotal role in orchestrating immune cell trafficking and initiating intracellular signaling. It is highly expressed on diverse leukocyte subsets—including skin‐resident T cells, mast cell progenitors and monocytes—and thereby directs targeted homing to peripheral tissues and the central nervous system. Engagement of SELPLG initiates intracellular cascades through its association with adaptor molecules (such as the ERM proteins and the tyrosine kinase Syk), allowing it not only to mediate physical adhesion but also to function as an immunoregulatory receptor. Moreover, distinct glycoforms of SELPLG—such as those decorated with the cutaneous lymphocyte‐associated antigen (CLA)—enhance tissue‐specific recruitment, and its surface expression is modulated by inflammatory cytokines."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSELPLG also functions as a receptor for pathogens, thereby influencing viral tropism and host susceptibility. Multiple studies have demonstrated that enterovirus 71 exploits the N‐terminal region of SELPLG—with its requisite tyrosine-sulfated residues—to gain entry into leukocytes in a strain‐dependent manner. In parallel, SELPLG has been implicated in mediating intrinsic resistance against HIV, as its incorporation into viral particles and subsequent targeting by viral accessory proteins modulate infectivity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in adhesion and pathogen interactions, SELPLG contributes to thrombosis, cancer metastasis, and the modulation of therapeutic cell adhesion. Its expression on leukocyte‐derived microparticles helps localize procoagulant factors at sites of vascular injury, thereby triggering platelet activation. Aberrant SELPLG expression, genetic variations and even gene amplification have been linked to increased tumor cell adhesion, enhanced metastatic dissemination (including in multiple myeloma, non‐Hodgkin lymphoma, and solid tumors) and resistance to therapeutics. Proteolytic processing by enzymes such as BACE1 and bacterial proteases—as well as binding interactions with extracellular matrix components like versican—further modulate its adhesive and signaling functions, underscoring its multifaceted role in both inflammatory and neoplastic pathophysiology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "33", "end_ref": "48"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Bryan T Marshall, Mian Long, James W Piper, et al. 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