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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/175394
Structural and Functional Evolution of Glucose Transporter 4 (GLUT4): A Look at GLUT4 in Fish
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The insulin-responsive glucose transporter GLUT4 was first described in 1988 as a result of
studies on the regulation of glucose metabolism by insulin [1]. Soon after the discovery of
GLUT4, several groups cloned GLUT4 in the human [2], rat [3,4] and mouse [5]. Since its
discovery, GLUT4 has received, together with GLUT1, more experimental attention than any
other single membrane transport protein. Structurally, GLUT4 follows the predicted model
for class I glucose transporters. GLUT4 has a high affinity for glucose, with a Km of
approximately 5 mM [6], and also transports mannose, galactose, dehydroascorbic acid and
glucosamine [7-10]. In mammals, GLUT4 is mainly expressed in cardiac and skeletal muscle,
brown and white adipose tissue, and brain [6,11,12]. GLUT4 plays a pivotal role in whole
body glucose homeostasis, mediating the uptake of glucose regulated by insulin [13,14].
GLUT4 is responsible for the reduction in the postprandial rise in plasma glucose levels [6].
Insulin acts by stimulating the translocation of specific GLUT4-containing vesicles from
intracellular stores to the plasma membrane (PM) resulting in an immediate increase in
glucose transport [6,15]. The disruption of GLUT4 expression has been extensively associated
with pathologies of impaired glucose uptake and insulin resistance such as type 2 diabetes
and obesity [13,16-18]...
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MARÍN JUEZ, Rubén, et al. Structural and Functional Evolution of Glucose Transporter 4 (GLUT4): A Look at GLUT4 in Fish. Chapter 2 in: Szablewski. Leszek. 2014. Glucose Homeostasis. IntechOpen. ISBN: 978-953-51-7212-3. DOI: 10.5772/57190. pp: 37-67.. [consulted: 17 of October of 2026]. Available at: https://hdl.handle.net/2445/175394