{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSOAT1 (also known as ACAT1) is an integral, endoplasmic reticulum–resident enzyme that catalyzes the esterification of free cholesterol with long‐chain fatty acyl–coenzyme A to produce cholesteryl esters, which are then stored in cytosolic lipid droplets. Extensive biochemical and structural studies have revealed that SOAT1 possesses a unique architecture composed of nine transmembrane domains and displays a high degree of stereospecificity in substrate recognition. These basic functions underpin its critical role in maintaining intracellular cholesterol homeostasis, regulating lipoprotein assembly, and modulating lipid storage in a wide range of cell types and tissues."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of cancer, dysregulated SOAT1 activity has emerged as a key driver of aberrant cholesterol metabolism that supports tumor cell survival and proliferation. In glioblastoma, for example, SOAT1‐mediated conversion of endoplasmic reticulum cholesterol into inert cholesteryl esters is necessary for sustained SREBP‑1 activation and lipogenesis, so that its inhibition effectively suppresses tumor growth. Similarly, in adrenocortical carcinoma, pharmacological blockade of SOAT1 by agents such as mitotane leads to toxic accumulation of free cholesterol and oxysterols accompanied by endoplasmic reticulum stress and impaired steroidogenesis. In prostate, ovarian, and pancreatic ductal adenocarcinoma cells, altered SOAT1 expression correlates with aggressive disease phenotypes and identifies the enzyme as an attractive target for antitumor therapies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "33", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond oncology, SOAT1’s regulation of cholesterol esterification plays a pivotal role in neurodegenerative and metabolic disorders. In neuronal models, excessive esterification of oxysterols such as 24(S)‐hydroxycholesterol triggers the formation of abnormal lipid droplet–like structures that contribute to cell death, while inhibition of SOAT1 enhances autophagic clearance of toxic amyloid‑β peptides, implicating the enzyme in Alzheimer’s disease pathology. Moreover, in macrophages, SOAT1 governs the balance between free cholesterol and cholesteryl esters, thereby influencing foam cell formation—a critical step in atherosclerosis—and modulating inflammatory responses associated with hyperlipidemia and cardiovascular disease. Such diverse roles underscore SOAT1’s function as a central node in lipid homeostasis and its promise as a therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "39", "end_ref": "43"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Yi Zhang, Chunjiang Yu, Jay Liu, et al. 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