# name
Structural and Functional Evolution of Glucose Transporter 4 (GLUT4): A Look at GLUT4 in Fish

# metadata.dc.description.abstract[].value
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]...

# metadata.dc.rights[].value
cc by (c) Marín Juez, Rubén et al., 2014

# metadata.dc.source[].value
Llibres / Capítols de llibre (Biologia Cel·lular, Fisiologia i Immunologia)

# metadata.dc.title[].value
Structural and Functional Evolution of Glucose Transporter 4 (GLUT4): A Look at GLUT4 in Fish