{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nS100A10 (also known as p11) is a multifunctional protein that, by forming a tight heterotetramer with annexin A2, governs key extracellular proteolytic events. The A2t complex binds tissue‐plasminogen activator and plasminogen through molecular determinants (including carboxyl‐terminal lysines of S100A10), thereby locally enhancing plasmin generation that is essential for fibrinolysis. In normal physiology this mechanism aids in vascular homeostasis, yet in pathological conditions – such as in acute promyelocytic leukemia, where its upregulation accentuates excessive fibrinolysis, or in diverse cancers (colorectal, pancreatic, renal, and others) – increased S100A10 expression promotes extracellular matrix degradation, cell invasion, and metastasis. Moreover, its intracellular stability is critically maintained by annexin A2, which protects S100A10 from ubiquitin‐dependent degradation, while post‐translational modifications further modulate its activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its role in proteolysis, the annexin A2/S100A10 complex orchestrates multiple aspects of membrane trafficking and pathogen entry. High‐risk human papillomaviruses exploit the complex by engaging S100A10 via a specific L2‐ protein epitope, a step that is critical for viral internalization and intracellular transport. Similarly, studies in bacterial invasion models (e.g. Salmonella) implicate the complex in facilitating pathogen uptake. Moreover, the localization and activity of the complex at the plasma membrane are finely regulated by cellular cues such as pH shifts, phosphorylation, and lipid interactions – features that are equally important during exocytotic events (for example, the release of von Willebrand factor) and in signaling responses to lipid mediators like ceramide 1‐phosphate."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles at the cell surface, S100A10 critically influences neuronal signaling and behavioral responses. In the central nervous system S100A10 regulates the trafficking and cell surface expression of serotonin 1B receptors, thereby modulating serotonergic transmission and contributing to antidepressant-like effects. Altered p11 expression is observed in depressive states and in related conditions such as irritable bowel syndrome and Parkinson’s disease with comorbid depression, and genetic variations within this regulatory axis (which intersects with tPA/plasminogen-mediated conversion of pro–brain-derived neurotrophic factor) have been linked to differential treatment responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional work has highlighted S100A10’s involvement in diverse cellular regulatory processes. It participates in the trafficking and membrane targeting of ion channels such as TASK‐1 and CFTR, thus influencing resting membrane potentials and epithelial ion transport. S100A10 also interacts with the scaffold protein AHNAK, and its aberrant expression is noted in a range of neoplasms – from thyroid and melanocytic tumors to ovarian cancers – where it serves as a potential biomarker of aggressive behavior. Moreover, its dynamic engagement with membrane phospholipids and integration into multiprotein complexes underscore a broader role as a molecular chaperone that adapts its functions to cellular context and external stimuli."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "28", "end_ref": "37"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Andrew R Beaton, Javier Rodriguez, Y Krishnamohan Reddy, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.192432299"}], "href": "https://doi.org/10.1073/pnas.192432299"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12235365"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12235365"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Travis J MacLeod, Mijung Kwon, Nolan R Filipenko, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phospholipid-associated annexin A2-S100A10 heterotetramer and its subunits: characterization of the interaction with tissue plasminogen activator, plasminogen, and plasmin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M301017200"}], "href": "https://doi.org/10.1074/jbc.M301017200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12730231"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12730231"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Mijung Kwon, Travis J MacLeod, Yi Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Front Biosci (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2741/1529"}], "href": "https://doi.org/10.2741/1529"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15574370"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15574370"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Mijung Kwon, Chang-Soon Yoon, Woojin Jeong, et al. 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