Compartment-ablation studies of GLUT4 distribution in adipocytes: evidence for multiple intracellular pools.
The available data suggest that GLUT4 does populate the recycling endosomal system to some extent, but that a large proportion of the intracellular GLUT4 resides in a compartment that is devoid of transferrin receptors and may have properties more akin to specialized secretory vesicles. The study of the nature and biogenesis of this compartment will provide important insight into the mechanism by which insulin stimulates glucose transport. Further study of the role of the synaptobrevins in these distinct subcellular compartments will probably shed further light on the mechanism by which insulin stimulates GLUT4 translocation.
Millar
C A
CA
Division of Biochemistry and Molecular Biology, University of Glasgow, Scotland, U.K.
Campbell
L C
LC
Cope
D L
DL
Melvin
D R
DR
Powell
K A
KA
Gould
G W
GW
D017667:Adipocytes / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D003594:Cytoplasmic Granules / Q000378:metabolism / Q000648:ultrastructure; D011992:Endosomes / Q000378:metabolism / Q000648:ultrastructure; D051275:Glucose Transporter Type 4; D008565:Membrane Proteins / Q000032:analysis; D016253:Microscopy, Immunoelectron; D009004:Monosaccharide Transport Proteins / Q000032:analysis / Q000378:metabolism*; D009124:Muscle Proteins; D009419:Nerve Tissue Proteins / Q000032:analysis; D015388:Organelles / Q000378:metabolism* / Q000648:ultrastructure; D050683:R-SNARE Proteins; D013572:Synaptic Vesicles / Q000378:metabolism
D051275:Glucose Transporter Type 4; D008565:Membrane Proteins; D009004:Monosaccharide Transport Proteins; D009124:Muscle Proteins; D009419:Nerve Tissue Proteins; D050683:R-SNARE Proteins