{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMUC1 is a transmembrane glycoprotein that is normally present in epithelial cells but becomes overexpressed and aberrantly glycosylated in many human carcinomas. This tumor‐associated MUC1 exhibits altered biochemical properties and cellular distribution that allow it to engage in oncogenic signal transduction. In particular, MUC1 influences gene expression at both transcriptional and post‐transcriptional levels and interacts with regulatory proteins such as p53 and β‑catenin – thereby promoting cellular transformation and contributing to disease progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMUC1 also functions as a key mediator of cellular resistance to apoptosis. By localizing to mitochondria – a process that involves direct interactions with cytoplasmic chaperones – MUC1 interferes with the release of apoptogenic factors and reduces caspase activation in response to DNA damage. This anti‐apoptotic activity enables tumor cells to survive genotoxic stress and contributes to chemoresistance."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMUC1 contributes to the epithelial‐to‐mesenchymal transition (EMT), invasion, and metastasis of tumor cells. Through its cytoplasmic tail, MUC1 alters cellular adhesion by modulating interactions with key ligands and by partnering with signaling molecules that regulate EMT markers. In addition, by affecting the display of adhesion molecules on the cell surface, MUC1 promotes motility, facilitates cell aggregation, and enhances metastatic dissemination."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its direct role in tumor cell biology, MUC1 has emerged as an important modulator of antitumor immune responses and a promising target for immunotherapy. Its aberrant glycoforms are being exploited for the development of chimeric antigen receptor (CAR)–grafted T cells and vaccine strategies, while MUC1 also regulates immune checkpoint molecules such as PD‑L1, thereby contributing to tumor immune escape."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in cancer, MUC1 is integral to mucosal defense and epithelial homeostasis. Its extracellular domain—also known as KL‑6 when shed into circulation—serves as a clinical biomarker in interstitial lung diseases. Additionally, in the gastrointestinal and uterine epithelia, MUC1 functions as a releasable decoy that limits microbial adhesion (for example, during Helicobacter pylori infection) and helps maintain barrier integrity during tissue regeneration."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPost‐translational processing of MUC1 is central to its multifaceted functions. Autoproteolytic cleavage within its SEA domain and alternative splicing generate different MUC1 isoforms with distinct biological activities. These structural variants not only influence intracellular trafficking and interactions with regulatory proteins but also affect the repertoire of O–glycosylation patterns, which in turn modulate both the adhesive and signaling properties of MUC1."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, the multifarious signaling roles of MUC1 render it a valuable biomarker and therapeutic target in cancer. Through modulation of metabolic pathways, regulation of cell–cell aggregation, and interactions with diverse signaling complexes, MUC1 integrates various processes that support tumor growth, survival, and dissemination. Efforts to target its oncogenic functions – ranging from small molecule inhibitors and peptide blockers to immunotherapeutic strategies – underscore MUC1’s clinical significance as an integrative mediator of tumor progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "33", "end_ref": "41"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Sritama Nath, Pinku Mukherjee "}, {"type": "b", "children": [{"type": "t", "text": "MUC1: a multifaceted oncoprotein with a key role in cancer progression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Trends Mol Med (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molmed.2014.02.007"}], "href": "https://doi.org/10.1016/j.molmed.2014.02.007"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24667139"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24667139"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Sandra Guaita, Isabel Puig, Clara Franci, et al. 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