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Emerging role for AS160/TBC1D4 and TBC1D1 in the regulation of GLUT4 traffic.
- K. Sakamoto, G. Holman
- Biology, MedicineAmerican journal of physiology. Endocrinology and…
- 1 July 2008
The current state of a hypothesis that suggests that phosphorylation of the Rab-GTPase-activating proteins leads to increased GTP loading of Rab proteins on GLUT4 vesicles and subsequently to increased interaction with Rab effectors that control GLUT 4 vesicle translocation is examined.
The glucose transporter family: structure, function and tissue-specific expression.
The facilitative glucose transporters are specific for the D-enantiomer of glucose and are not coupled to any energy-requiring components, such as ATP hydrolysis or a HI gradient.
Contraction stimulates translocation of glucose transporter GLUT4 in skeletal muscle through a mechanism distinct from that of insulin.
- S. Lund, G. Holman, O. Schmitz, O. Pedersen
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 20 June 1995
Contraction-mediated translocation of the GLUT4 transporters to the cell surface was closely correlated with the glucose transport activity and could account fully for the increment in glucose uptake after contraction.
The causal role of breakfast in energy balance and health: a randomized controlled trial in lean adults1234
- J. Betts, J. D. Richardson, E. Chowdhury, G. Holman, K. Tsintzas, D. Thompson
- MedicineThe American journal of clinical nutrition
- 4 June 2014
Daily breakfast is causally linked to higher physical activity thermogenesis in lean adults, with greater overall dietary energy intake but no change in resting metabolism.
Blood—Brain Barrier Glucose Transporter
Results show that hypoglycemia, but not hyperglycemi, alters glucose transport activity at the BBB and that these changes in transport activity result from both an overall increase in total BBB GLUT1 and an increased transporter concentration at the luminal surface.
Identification of Mammalian Vps24p as an Effector of Phosphatidylinositol 3,5-Bisphosphate-dependent Endosome Compartmentalization*
- P. Whitley, Barbara J. Reaves, M. Hashimoto, A. M. Riley, B. Potter, G. Holman
- Biology, MedicineJournal of Biological Chemistry
- 3 October 2003
The use of cDNA phage libraries in conjunction with synthetic biotinylated derivatives of phosphatidylinositol 3,5-bisphosphate in the identification of a mammalian phosphate-binding protein, mVps24p, is reported, providing the first direct link between phosphate-based lipid found in eukaryotes and the protein machinery involved in the production of the class-E cellular phenotype.
Structural requirements for binding to the sugar-transport system of the human erythrocyte.
The structural requirements for binding to the glucose/sorbose-transport system in the human erythrocyte were explored by measuring the inhibition constants, K(i), for specifically substituted…
The human glomerular podocyte is a novel target for insulin action.
Novel conditionally immortalized human podocytes in vitro and human glomeruli ex vivo are reported that the podocyte, the principal cell responsible for prevention of urinary protein loss, is insulin responsive and able to approximately double its glucose uptake within 15 min of insulin stimulation.
Moving the insulin-regulated glucose transporter GLUT4 into and out of storage.
Investigations of the composition and structure of the GLUT4 storage compartment, together with the targeting motifs that directGLUT4 to this compartment, have been extensive but have been controversial, and a clearer consensus of opinion is provided on the mechanisms involved in the formation of this storage compartment.
Cell surface labeling of glucose transporter isoform GLUT4 by bis-mannose photolabel. Correlation with stimulation of glucose transport in rat adipose cells by insulin and phorbol ester.
- G. Holman, I. Kozka, +5 authors S. Cushman
- Biology, MedicineThe Journal of biological chemistry
- 25 October 1990
GLUT4 is the major glucose transporter isoform under all conditions, and it is selectively and markedly enriched in response to insulin but not PMA which increases GLUT1 and GLUT4 equally.