ArticleThe Journal of cell biology1994
The amino terminus of GLUT4 functions as an internalization motif but not an intracellular retention signal when substituted for the transferrin receptor cytoplasmic domain.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 78 citations in OpenAlex.
- SNARE-binding protein synaptosomal-associated protein of 29 kDa (SNAP29) regulates the intracellular sequestration of glucose transporter 4 (GLUT4) vesicles in adipocytes.Journal of diabetes investigation · 2023Article
- Cryo-EM structure of human glucose transporter GLUT4.Nature communications · 2022Article
- Effects of physical exercise on muscle metabolism and meat quality characteristics of Mongolian sheep.Food science & nutrition · 2022Article
- Functional Characterization of Facilitative Glucose Transporter 4 With a Delay Responding to Plasma Glucose Level in Blunt Snout Bream (Frontiers in physiology · 2020Article
- Thirty sweet years of GLUT4.The Journal of biological chemistry · 2019Review
- Ankyrin-B metabolic syndrome combines age-dependent adiposity with pancreatic β cell insufficiency.The Journal of clinical investigation · 2015Article
- Reciprocal regulation of endocytosis and metabolism.Cold Spring Harbor perspectives in biology · 2014Review
- High basal cell surface levels of fish GLUT4 are related to reduced sensitivity of insulin-induced translocation toward GGA and AS160 inhibition in adipocytes.American journal of physiology. Endocrinology and metabolism · 2010Article
- Functional roles of short sequence motifs in the endocytosis of membrane receptors.Frontiers in bioscience (Landmark edition) · 2009Review
- The C-terminus of GLUT4 targets the transporter to the perinuclear compartment but not to the insulin-responsive vesicles.The Biochemical journal · 2009Article
- Molecular mechanisms controlling GLUT4 intracellular retention.Molecular biology of the cell · 2008Article
- Identification of amino acid residues within the C terminus of the Glut4 glucose transporter that are essential for insulin-stimulated redistribution to the plasma membrane.The Journal of biological chemistry · 2008Article
- Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates Glut4 trafficking in adipocytes.Cell metabolism · 2007Article
- GLUT4 is internalized by a cholesterol-dependent nystatin-sensitive mechanism inhibited by insulin.The EMBO journal · 2006Article
- GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in Syntaxins 6 and 16 but not TGN38: involvement of an acidic targeting motif.Molecular biology of the cell · 2003Article
- SARA, a FYVE domain protein, affects Rab5-mediated endocytosis.Journal of cell science · 2002Article
- Multiple endocytic signals in the C-terminal tail of the cystic fibrosis transmembrane conductance regulator.The Biochemical journal · 2001Article
- A di-leucine sequence and a cluster of acidic amino acids are required for dynamic retention in the endosomal recycling compartment of fibroblasts.Molecular biology of the cell · 2001Article
- The cytosolic C-terminus of the glucose transporter GLUT4 contains an acidic cluster endosomal targeting motif distal to the dileucine signal.The Biochemical journal · 2000Article
- GLUT4 and transferrin receptor are differentially sorted along the endocytic pathway in CHO cells.The Journal of cell biology · 1998Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Previous studies have demonstrated that the amino-terminal cytoplasmic domain of GLUT4 contains a phenylalanine-based targeting motif that determines its steady state distribution between the surface and the interior of cells (Piper, R. C., C. Tai, P. Kuleza, S. Pang, D. Warnock, J. Baenziger, J. W. Slot, H. J. Geuze, C. Puri, and D. E. James. 1993. J. Cell Biol. 121:1221). To directly measure the effect that the GLUT4 amino terminus has on internalization and subsequent recycling back to the cell surface, we constructed chimeras in which this sequence was substituted for the amino-terminal cytoplasmic domain of the human transferrin receptor. The chimeras were stably transfected into Chinese hamster ovary cells and their endocytic behavior characterized. The GLUT4-transferrin receptor chimera was recycled back to the cell surface with a rate similar to the transferrin receptor, indicating that the GLUT4 sequence was not promoting intracellular retention of the chimera. The GLUT4-transferrin receptor chimera was internalized at half the rate of the transferrin receptor. Substitution of an alanine for phenylalanine at position 5 slowed internalization of the chimera by twofold, to a level characteristic of bulk membrane internalization. However, substitution of a tyrosine increased the rate of internalization to the level of the transferrin receptor. Neither of these substitutions significantly altered the rate at which the chimeras were recycled back to the cell surface. These results demonstrate that the major function of the GLUT4 amino-terminal domain is to promote the effective internalization of the protein from the cell surface, via a functional phenylalanine-based internalization motif, rather than retention of the transporter within intracellular structures.
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