Molecular Basis of Insulin-stimulated GLUT4 Vesicle Trafficking

Pessin, Jeffrey E.; Thurmond, Debbie C.; Elmendorf, Jeffrey S.; Coker, Kenneth J.; Okada, Shuichi

doi:10.1074/jbc.274.5.2593

Cited by 384 publications

(319 citation statements)

References 82 publications

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“…The fidelity of this process is mediated at least in part by SNARE proteins [27]. In adipocytes and muscle, the SNAREs syntaxin 4 and VAMP2 have been identified as being of crucial importance in insulin-stimulated GLUT4 translocation [7,12,28,29].…”

Section: Discussionmentioning

confidence: 99%

Reduced insulin-stimulated GLUT4 bioavailability in stroke-prone spontaneously hypertensive rats

et al. 2005

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Aims/hypothesis: Insulin-stimulated glucose transport is impaired in a genetic model of hypertension, the stroke-prone spontaneously hypertensive rat (SHRSP), yet the molecular mechanisms that underlie this defect in the animals remain unclear. Methods: We examined the effects of insulin on the trafficking of the insulin-responsive glucose transporter GLUT4 to the plasma membrane in isolated adipocytes from SHRSP and normotensive control WistarKyoto (WKY) rats. Results: Treatment of isolated adipocytes with insulin resulted in trafficking of GLUT4 to the plasma membrane. There was no significant difference in the magnitude of insulin-stimulated GLUT4 trafficking from intracellular membranes to the plasma membrane between strains. In contrast, we demonstrated that there is a significant reduction in GLUT4 accessible to the glucose photolabel Bio-LC-ATB-BGPA at the plasma membrane of SHRSP adipocytes compared with control rats. Conclusions/ interpretation: We propose that a large proportion of GLUT4 translocated to the plasma membrane in response to insulin is not able to bind substrate and catalyse transport in the SHRSP. Therefore, there is a reduction in bioavailable GLUT4 in SHRSP animals that is likely to account, at least in part, for the reduced insulin-stimulated glucose uptake.

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Section: Discussionmentioning

confidence: 99%

Reduced insulin-stimulated GLUT4 bioavailability in stroke-prone spontaneously hypertensive rats

et al. 2005

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“…In the basal state, GLUT4 undergoes a slow but continuous recycling between the plasma membrane and several intracellular compartments, with only 5% of the total GLUT4 protein pool localized to the plasma membrane. In response to acute insulin stimulation (2-3 min), however, the rate of GLUT4 exocytosis markedly increases concomitant with a small decrease in endocytosis, so that approximately 50% of the GLUT4 protein are relocated to the cell surface [1,4,5]. The rate of exocytosis subsequently decreases following the removal of the insulin signal, and this trafficking system returns back to the basal condition.…”

Section: Introductionmentioning

confidence: 99%

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Hou

Pessin

2007

Current Opinion in Cell Biology

132

116

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SummaryGlucose transporter 4 (GLUT4) is the major insulin regulated glucose transporter expressed mainly in muscle and adipose tissue. GLUT4 is stored in a poorly characterized intracellular vesicular compartment and translocates to the cell surface in response to insulin stimulation resulting in increase glucose uptake. This process is essential for the maintenance of normal glucose homeostasis and involves a complex interplay of trafficking events and intracellular signaling cascades. Recent studies have identified sortilin as an essential element for the formation of GLUT4 storage vesicles during adipogenesis and GGA (Golgi-localized γ-ear-containing Arf-binding protein) as a key coat adaptor for the entry of newly synthesized GLUT4 into the specialized compartment. Insulinstimulated GLUT4 translocation from this compartment to the plasma membrane appears to require the Akt/protein kinase B substrate, termed AS160 (Akt Substrate of 160 kDa). In addition, the VPS9 domain-containing protein Gapex-5 in complex with CIP4 appears to function as a Rab31 guanylnucleotide exchange factor that is necessary for insulin-stimulated GLUT4 translocation. Here we attempt to summaries recent advances in GLUT4 vesicle biogenesis, intracellular trafficking and membrane fusion.

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“…Insulin stimulates relocalization of the GLUT4 glucose transporter to the cell surface. Before reception of the signal, the GLUT4 receptor is enriched in intracellular vesicles (reviewed by Pessin et al, 1999). The redistribution of GLUT4 appears to be a case of regulated exocytosis, as occurs during synaptic vesicle fusion; it may also involve the selective retention of the transporter within a distinct intracellular compartment.…”

Section: Yl Localizationmentioning

confidence: 99%

Regulation of the Vitellogenin Receptor duringDrosophila melanogasterOogenesis

Schonbaum

Perrino

Mahowald

2000

MBoC

104

115

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In many insects, development of the oocyte arrests temporarily just before vitellogenesis, the period when vitellogenins (yolk proteins) accumulate in the oocyte. Following hormonal and environmental cues, development of the oocyte resumes, and endocytosis of vitellogenins begins. An essential component of yolk uptake is the vitellogenin receptor. In this report, we describe the ovarian expression pattern and subcellular localization of the mRNA and protein encoded by the Drosophila melanogaster vitellogenin receptor gene yolkless (yl). yl RNA and protein are both expressed very early during the development of the oocyte, long before vitellogenesis begins. RNA in situ hybridization and lacZ reporter analyses show that yl RNA is synthesized by the germ line nurse cells and then transported to the oocyte. Yl protein is evenly distributed throughout the oocyte during the previtellogenic stages of oogenesis, demonstrating that the failure to take up yolk in these early stage oocyte is not due to the absence of the receptor. The transition to the vitellogenic stages is marked by the accumulation of yolk via clathrin-coated vesicles. After this transition, yolk protein receptor levels increase markedly at the cortex of the egg. Consistent with its role in yolk uptake, immunogold labeling of the receptor reveals Yl in endocytic structures at the cortex of wild-type vitellogenic oocytes. In addition, shortly after the inception of yolk uptake, we find multivesicular bodies where the yolk and receptor are distinctly partitioned. By the end of vitellogenesis, the receptor localizes predominantly to the cortex of the oocyte. However, during oogenesis in yl mutants that express full-length protein yet fail to incorporate yolk proteins, the receptor remains evenly distributed throughout the oocyte. INTRODUCTIONThe magnitude of yolk uptake into the oocyte during vitellogenesis suggests a heavy involvement of the endocytic machinery; indeed, the clathrin-coated vesicle was originally described in the vitellogenic mosquito oocyte (Roth and Porter, 1964). Because the morphological features are so striking, descriptions of vitellogenesis have been made in a broad range of oviparous species, including birds (Perry and Gilbert, 1979;Perry et al., 1984), frogs (Opresko and Wiley, 1987;Wall and Patel, 1987), fish (reviewed by Wallace andSelman, 1990), and insects (Cummings andMahowald, 1972; Giorgi and Jacob, 1977a,b;Raikhel, 1984;van Antwerpen et al., 1993) (reviewed by Raikhel and Dhadialla, 1992). In several cases, immunocytochemical and ultrastructural studies using labeled yolk protein precursors or fluid phase markers have followed the fate of the proteins as they are sorted to the yolk platelets (Giorgi and Jacob, 1977a;Raikhel, 1984;Busson et al., 1989). The initial steps in the yolk uptake pathway are similar to those described for general receptor-mediated endocytosis (Goldstein et al., 1985;Mukherjee et al., 1997). Vitellogenins (Vgs) are taken up through clathrin-coated pits, and they accumulate initially in vesiculotubul...

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Molecular Basis of Insulin-stimulated GLUT4 Vesicle Trafficking

Cited by 384 publications

References 82 publications

Reduced insulin-stimulated GLUT4 bioavailability in stroke-prone spontaneously hypertensive rats

Reduced insulin-stimulated GLUT4 bioavailability in stroke-prone spontaneously hypertensive rats

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Regulation of the Vitellogenin Receptor duringDrosophila melanogasterOogenesis

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