{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMGLL (monoacylglycerol lipase) plays a central role in cancer‐related metabolic reprogramming. In aggressive tumors – including prostate, colorectal, nasopharyngeal, hepatocellular, and glioblastoma – elevated MGLL activity liberates free fatty acids from monoacylglycerols, which in turn fuel oncogenic lipid networks that promote cell migration, invasion, and tumor growth. In some contexts, however, diminished MGLL expression has been linked to aberrant activation of the PI3K–Akt pathway, suggesting that MGLL’s lipid‐modulatory functions may also act as a brake on tumor cell proliferation. Moreover, in the tumor microenvironment MGLL expression in macrophages appears to shift inflammatory signaling pathways (for example, via CB2/TLR4 or PGE₂ production) that impact both tumor progression and the cancer cell–immune cell interplay."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the nervous system and other non‐tumoral tissues, MGLL is the principal enzyme that degrades the endocannabinoid 2‐arachidonoylglycerol (2‑AG), thereby modulating cannabinoid receptor signaling and synaptic transmission. MGLL‐mediated hydrolysis of 2‑AG is critical for maintaining endocannabinoid tone during neurodevelopment and in response to cellular redox changes – for example, via H₂O₂–induced sulfenylation – and alterations in MGLL levels have been implicated in conditions ranging from substance use disorders to altered white matter microstructure in chronic cannabis users. Such findings highlight MGLL’s multifaceted role in regulating lipid messengers that influence neural as well as peripheral homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nExtensive structural and mechanistic studies have elucidated the molecular architecture of MGLL. High‐resolution crystal structures and NMR analyses have revealed a large hydrophobic cavity with a flexible “lid” that undergoes conformational transitions to regulate substrate access to the catalytic serine residue. Detailed mapping of hydrogen‐bond networks and allosteric sites – including key regulatory residues – has provided insight into how point mutations or covalent inhibitors modulate the equilibrium between active and inactive states. These findings not only deepen our understanding of MGLL’s enzyme dynamics but also guide the development of selective inhibitors with promising therapeutic potential."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn parallel, genetic and population‐based studies have begun to unravel how rare variants and differential expression of MGLL contribute to broader metabolic and inflammatory diseases. Innovative analytic approaches have linked MGLL polymorphisms to altered endocannabinoid metabolism in obesity and related disorders, while additional investigations have underscored the importance of MGLL regulation in modulating cellular lipid profiles and systemic metabolic homeostasis. These studies collectively emphasize the translational potential of targeting MGLL not only in cancer and neurodegeneration but also in metabolic disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "30", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Daniel K Nomura, Jonathan Z Long, Sherry Niessen, et al. 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