{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSorcin (SRI) is emerging as a multifunctional calcium‐binding protein whose aberrant expression plays a central role in the development and progression of cancer. In numerous malignancies—including acute leukemias, colorectal, gastric, nasopharyngeal, breast, ovarian, and hepatocellular carcinomas—sorcin is markedly overexpressed and has been linked to the onset of multidrug resistance. By interacting with proteins such as the mitochondrial chaperone TRAP1 and regulators of Ca²⁺ homeostasis, sorcin modulates anti‐apoptotic pathways, stimulates drug efflux (via up‐regulation of P‐glycoprotein and related transporters), and supports the epithelial‐to‐mesenchymal transition and cancer stem cell characteristics that underlie tumor aggressiveness and metastasis. Moreover, sorcin expression correlates with poor clinical outcomes and advanced tumor stage, suggesting its potential as both a prognostic biomarker and a therapeutic target for overcoming chemoresistance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its oncogenic implications, sorcin is a key modulator of intracellular calcium dynamics in several non‐malignant settings. In the heart, studies in transgenic and adenovirus‐transfected models have demonstrated that sorcin regulates excitation–contraction coupling by modulating ryanodine receptor activity and L‐type calcium currents, thereby contributing to contractile function. In pancreatic β‐cells, sorcin sequesters transcription factors (such as ChREBP) in the cytosol in a Ca²⁺‐dependent manner, thus influencing glucose‐mediated gene expression. Its role in preserving endoplasmic reticulum Ca²⁺ levels and preventing ER stress is also evident in neurodegenerative conditions, where sorcin’s interaction with SERCA, ryanodine receptors, and other ER components appears to counteract the toxic effects of amyloid‐β and tau. Furthermore, sorcin contributes to the regulation of calcium sparks in vascular smooth muscle, underpinning its broader role as a calcium sensor and effector."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in calcium regulation and chemoresistance, sorcin is intricately involved in the fine‐tuning of intracellular signaling and cell cycle progression. It interacts with a range of regulatory proteins—from kinases such as PLK1 and Aurora family members to components implicated in the cAMP response element–binding (CREB) pathway—to modulate apoptosis, mitosis, and cytokinesis. These functions, which extend to controlling the expression of drug transporters and influencing the balance between pro‐ and anti‐apoptotic factors, reinforce sorcin’s status as a multifaceted intracellular mediator and a promising target for therapeutic intervention in both cancer and other diseases where calcium dysregulation is pathogenic."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "30", "end_ref": "37"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Guangyao Li, Yaohong Tan, Chunzheng Yang, et al. 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