{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nS100A2 is an EF‐hand calcium‐binding protein that exhibits dynamic subcellular localization and plays a pivotal role in mediating stress responses and tumor suppression. In several studies, S100A2 was shown to translocate from the cytoplasm to the nucleus following insult (for example, during recovery from hydroxyurea treatment), where it forms a Ca²⁺‐dependent complex with the tumor suppressor p53 that enhances its transcriptional activity. In addition, biophysical studies revealed that S100A2 binds Zn²⁺ with high affinity, suggesting that its responsiveness to intracellular Ca²⁺ signals may be modulated by zinc and that these regulatory mechanisms might impact its functions in DNA damage responses and keratinocyte differentiation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "Disruption or alteration of S100A2 expression has been implicated in the progression of several malignancies. In diverse tumor types—including non‐small cell lung cancer, esophageal and gastric adenocarcinomas—deregulated S100A2 levels have been correlated with tumor progression, metastasis and clinical outcome. In these contexts, S100A2 interacts with key regulatory proteins (such as p53 and its family members) and modulates signaling pathways including TGF‑β and PI3K/AKT. Such interactions can influence critical cellular processes such as epithelial–mesenchymal transition, metabolic reprogramming and cell cycle control. Thus, depending on tumor type and context, S100A2 may act either as a tumor suppressor or, in a paradoxical twist, support pro‐invasive signaling cascades that contribute to metastasis and poor prognosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "23"}]}, {"type": "t", "text": "Futhermore, beyond its roles in tumor biology, S100A2 is emerging as an important biomarker in non‐neoplastic settings. Altered S100A2 expression has been observed in conditions as diverse as wound healing and cutaneous adverse drug reactions, where its level and subcellular distribution serve as indicators of keratinocyte stress and tissue damage. Its involvement in the regulation of chaperone–mediated ubiquitination and oxidative stress responses reinforces its status as a multifunctional protein whose dysregulation may contribute not only to cancer progression (in malignancies such as laryngeal, oral and hepatic carcinomas) but also to perturbations in normal epithelial homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "36"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Andrea Mueller, Beat W Schäfer, Stefano Ferrari, et al. 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