{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSLC2A4, which encodes the GLUT4 protein, is the primary insulin‐responsive glucose transporter that governs the uptake of glucose into muscle and adipose cells. In the basal state, GLUT4 is sequestered in intracellular vesicles, but upon insulin stimulation it is rapidly mobilized and translocated to the plasma membrane, thereby facilitating efficient glucose disposal and maintaining systemic glucose homeostasis. Moreover, increased expression of GLUT4—as seen with strength training and exercise—enhances insulin sensitivity and can ameliorate insulin‐resistant states, while its overexpression in skeletal muscle has been shown to improve metabolic profiles. This central role of GLUT4 in insulin‐mediated glucose uptake has been demonstrated in studies ranging from muscle and adipose cell models to in vivo physiological investigations."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA complex network of signaling cascades and regulatory kinases tightly controls the intracellular trafficking, expression, and activity of GLUT4. Insulin activates the PI3K–Akt pathway along with downstream effectors (such as AS160 and TUG) to regulate both the exocytosis and retention of GLUT4‐containing vesicles. Various modulators, including MAP kinases, oxidative stress (as induced by overnutrition) and hormonal signals like leptin and estrogen, further tune GLUT4’s functional delivery at the cell surface. Importantly, perturbations in these pathways are linked not only to insulin resistance in conditions such as type 2 diabetes, gestational diabetes and polycystic ovary syndrome but also to aberrant GLUT4 localization in malignancies and other metabolic disorders, emphasizing its broad physiological and pathophysiological importance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to dynamic trafficking, GLUT4’s proper function depends on a cohort of auxiliary molecules that ensure its correct intracellular sorting, posttranslational modification, and transcriptional regulation. Proteins such as EHD1, Dennd4C, and Daxx have been implicated in the formation, perinuclear retention, and insulin‐stimulated recycling of GLUT4 vesicles, while structural modifications (for example, N‐glycosylation) are critical for its stability and accurate targeting. Transcription factors including MEF2, along with regulators like PGC-1 and LPIN1, modulate GLUT4 gene expression in response to metabolic and environmental cues. These multifaceted regulatory mechanisms are further influenced by pharmacological agents (metformin, phytochemicals), physiological stress, and even viral infections that switch glucose transporter profiles to meet altered cellular energy demands. Together, these findings underscore that modulation of GLUT4 trafficking and expression is central to metabolic adaptation and represents a promising target for therapeutic intervention in insulin resistance, diabetes, obesity, certain cancers, and other metabolic disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "47"}, {"type": "fg_f", "ref": "43"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Nia J Bryant, Roland Govers, David E James "}, {"type": "b", "children": [{"type": "t", "text": "Regulated transport of the glucose transporter GLUT4."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Rev Mol Cell Biol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nrm782"}], "href": "https://doi.org/10.1038/nrm782"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11994746"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11994746"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Mads K Holten, Morten Zacho, Michael Gaster, et al. 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