{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSLC2A1, encoding the facilitative glucose transporter GLUT1, is central to cellular glucose uptake via passive diffusion. Structural and mutational studies have revealed that GLUT1 adopts a canonical major facilitator superfamily fold with a central aqueous channel that alternates between inward‐ and outward‐facing conformations, thereby enabling efficient glucose transport. Posttranslational modifications such as S‐palmitoylation and regulation by insulin–Akt signals ensure appropriate plasma membrane localization and function, a feature that is also supported by crystallographic snapshots of the inward‐open conformation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn normal physiology, GLUT1 is indispensable for maintaining metabolic homeostasis in diverse tissues. In CD4(+) T lymphocytes, for example, GLUT1 expression is finely tuned to regulate the balance between metabolically glycolytic effector T cells and lipid‐dependent regulatory T cells, with its expression being modulated by factors such as TXNIP and even exploited as a receptor by viral glycoproteins. At barrier sites like the blood–brain barrier and in the placenta, GLUT1 ensures a continuous supply of glucose—critical for brain function and maternofetal nourishment. Moreover, genetic defects in SLC2A1 underlie GLUT1 deficiency syndrome, a condition characterized by low cerebrospinal fluid glucose, epilepsy, paroxysmal dyskinesias, and distinctive electroencephalographic abnormalities."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn cancer and other pathologic states, aberrant up‐regulation of GLUT1 fuels the elevated glycolytic rates—often referred to as the “Warburg Effect”—that support rapid proliferation and survival in hostile microenvironments. Elevated GLUT1 expression has been consistently documented in hepatocellular, endometrial, breast, lung, renal, and oral carcinomas, where it is often linked to activation of oncogenic signaling pathways like PI3K/AKT/mTOR. Furthermore, certain SLC2A1 mutations not only reduce glucose transport but can also confer a neomorphic ion conductance, contributing to paroxysmal movement disorders. In addition, altered GLUT1 function affects cellular bioenergetics as seen with the development of specific FRET‐based nanosensors that highlight its role in glucose flux."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its core metabolic role, GLUT1 has emerged as a promising clinical biomarker and therapeutic target. Its dysregulation contributes not only to tumor aggressiveness and altered energy metabolism in cancer—impacting tumor proliferation, invasion, and even the local immune landscape—but also to immune dysfunction as observed in leukemic contexts. Epigenetic regulators, including m6A RNA methylation, as well as differential expression patterns in leukocytes, further underscore the multifaceted regulatory landscape governing GLUT1 expression. Elevated GLUT1 levels have also been associated with diabetic complications and certain thyroid malignancies, emphasizing the broad clinical relevance of SLC2A1 dysregulation and the potential for targeted intervention."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "36", "end_ref": "41"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Dong Deng, Chao Xu, Pengcheng Sun, et al. 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