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Gene Review

Slc2a4  -  solute carrier family 2 (facilitated...

Rattus norvegicus

Synonyms: GLUT-4, Glucose transporter type 4, insulin-responsive, Glut-4, Glut4, Solute carrier family 2, facilitated glucose transporter member 4
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Disease relevance of Slc2a4


High impact information on Slc2a4


Chemical compound and disease context of Slc2a4


Biological context of Slc2a4

  • As the concentration required to significantly inhibit insulin-stimulated glucose uptake in primary rat adipocytes is well within the physiologic range achieved in therapy, we conclude that direct inhibition of Glut4 contributes to the insulin resistance observed in patients receiving this drug [9].
  • The mutated Glut4 was inhibited by pCMB or pCMBS and the IC50 of HgCl2 decreased to 47 microM, whereas K(m), substrate specificity and the sensitivity to cytochalasin B were not significantly changed, indicating that the existence of exofacial cysteine contributed only to increase SH sensitivity in Glut4 [10].
  • Phosphorylation of several vesicle proteins including Glut4 itself is rapidly activated by insulin [11].
  • H-raslys12-transformed brown adipocytes showed a 10-fold higher expression of Glut1 mRNA and protein than parental cells, Glut4 gene expression being completely down-regulated [12].
  • RESULTS: Compared with native insulin, the receptor binding activity of E,D-insulin was 31 %; the stimulating activity of E,D-insulin in glucose transport and lipogenesis were 45 % and 40 % respectively; the stimulations of Glut4 translocation and insulin receptor autophosphorylation of E,D-insulin were about 58 % and 46 % respectively [13].

Anatomical context of Slc2a4

  • Expression of a constitutively active, membrane-associated Akt-1 (PKB alpha) construct in 3T3L1 adipocytes was shown to induce glucose uptake in the absence of insulin by stimulating Glut4 translocation to the plasma membrane (Kohn, A. D., Summers, S. A., Birnbaum, M. J., and Roth, R. A. (1996) J. Biol. Chem. 271, 31372-31378) [14].
  • The distribution of Akt-2 in resting adipocytes was found to substantially overlap with that of Glut4 when light microsomes were subfractionated by a sucrose velocity gradient indicating possible co-localization [14].
  • The t1/2 values for ER to Golgi transit for Glut1 and Glut4 were < 1 and 24 h, respectively, in oocytes and approximately 5 and 20 min, respectively, in 3T3-L1 adipocytes [15].
  • Treatment of neonatal cardiac myocytes with the hypertrophic agonist 12-O-tetradecanoylphorbol-13-acetate or phenylephrine increased expression of Glut1 mRNA relative to Glut4 mRNA [16].
  • The rate of movement of the glucose transporter isoforms Glut1 and Glut4 from the endoplasmic reticulum (ER) to the Golgi apparatus was investigated by pulse labeling and monitoring endoglycosidase H resistance in mRNA-injected Xenopus oocytes and in 3T3-L1 adipocytes, a cell line that naturally expresses both transporter isoforms [15].

Associations of Slc2a4 with chemical compounds

  • Indinavir inhibits the glucose transporter isoform Glut4 at physiologic concentrations [9].
  • CONCLUSIONS: Indinavir appears to be a relatively selective inhibitor of the Glut4 isoform [9].
  • To examine the role of the exofacial cysteine, we replaced Met-455 of Glut4 (corresponding to Cys-429 of Glut1) with cysteine [10].
  • Pulse-chase in conjunction with sucrose density gradient analysis revealed that the rate-limiting step in the ER to Golgi processing of Glut4 was exit from the ER and not retention in an early Golgi compartment [15].
  • The GTBP70 binding to Glut4 was not affected by the presence of 2 mM EDTA, 2.4 mM Ca2+, or 150 mM K+ [17].

Physical interactions of Slc2a4

  • Akt-2 binds to Glut4-containing vesicles and phosphorylates their component proteins in response to insulin [11].

Co-localisations of Slc2a4


Other interactions of Slc2a4


Analytical, diagnostic and therapeutic context of Slc2a4

  • E2-stimulated changes in the steady state levels of messenger RNA (mRNA) and protein were measured for Glut1 and Glut4 by quantitative competitive RT-PCR and Western blots [23].
  • Simultaneous measurement of multiple mRNAs with a single control by quantitative competitive reverse transcriptase-polymerase chain reaction: glucose transporters Glut1 and Glut4 [24].
  • Theoretical considerations for extending the application of quantitative competitive polymerase chain reaction (qc-PCR) to include the simultaneous measurement of multiple mRNAs, specifically the mammalian glucose transporters Glut1 and Glut4, are presented with experimental data in which the accuracy and flexibility of the system are examined [24].
  • This study was performed to evaluate at the light microscopy level the expression of Glut-4 and Glut-1 transporters in normal and denervated diaphragm by immunohistochemistry method with specific Gluts antibodies [25].
  • These data indicated that (1) Glut-4 and Glut-1 transporters were observed in diaphragm; and (2) there were alterations in the expression of both glucose transporters after denervation [25].


  1. Regulation of glucose transport and transporter 4 (GLUT-4) in muscle and adipocytes of sucrose-fed rats: effects of N-3 poly- and monounsaturated fatty acids. Peyron-Caso, E., Fluteau-Nadler, S., Kabir, M., Guerre-Millo, M., Quignard-Boulangé, A., Slama, G., Rizkalla, S.W. Horm. Metab. Res. (2002) [Pubmed]
  2. Divergent regulation of the Glut 1 and Glut 4 glucose transporters in isolated adipocytes from Zucker rats. Pedersen, O., Kahn, C.R., Kahn, B.B. J. Clin. Invest. (1992) [Pubmed]
  3. Effect of maternal diabetes upon fetal rat myocardial and skeletal muscle glucose transporters. Schroeder, R.E., Doria-Medina, C.L., Das, U.G., Sivitz, W.I., Devaskar, S.U. Pediatr. Res. (1997) [Pubmed]
  4. Mechanisms regulating skeletal muscle glucose metabolism in sepsis. Vary, T.C., Drnevich, D., Jurasinski, C., Brennan, W.A. Shock (1995) [Pubmed]
  5. Intra-uterine growth restriction differentially regulates perinatal brain and skeletal muscle glucose transporters. Sadiq, H.F., Das, U.G., Tracy, T.F., Devaskar, S.U. Brain Res. (1999) [Pubmed]
  6. Regulated exocytosis: a novel, widely expressed system. Borgonovo, B., Cocucci, E., Racchetti, G., Podini, P., Bachi, A., Meldolesi, J. Nat. Cell Biol. (2002) [Pubmed]
  7. Preferential activation of microsomal diacylglycerol/protein kinase C signaling during glucose treatment (De Novo phospholipid synthesis) of rat adipocytes. Farese, R.V., Standaert, M.L., Arnold, T.P., Yamada, K., Musunuru, K., Hernandez, H., Mischak, H., Cooper, D.R. J. Clin. Invest. (1994) [Pubmed]
  8. Effects of gestational hypoxia on mRNA levels of Glut3 and Glut4 transporters, hypoxia inducible factor-1 and thyroid hormone receptors in developing rat brain. Royer, C., Lachuer, J., Crouzoulon, G., Roux, J., Peyronnet, J., Mamet, J., Pequignot, J., Dalmaz, Y. Brain Res. (2000) [Pubmed]
  9. Indinavir inhibits the glucose transporter isoform Glut4 at physiologic concentrations. Murata, H., Hruz, P.W., Mueckler, M. AIDS (2002) [Pubmed]
  10. Characterization of rat Glut4 glucose transporter expressed in the yeast Saccharomyces cerevisiae: comparison with Glut1 glucose transporter. Kasahara, T., Kasahara, M. Biochim. Biophys. Acta (1997) [Pubmed]
  11. Akt-2 binds to Glut4-containing vesicles and phosphorylates their component proteins in response to insulin. Kupriyanova, T.A., Kandror, K.V. J. Biol. Chem. (1999) [Pubmed]
  12. H-ras induces glucose uptake in brown adipocytes in an insulin- and phosphatidylinositol 3-kinase-independent manner. Valverde, A.M., Navarro, P., Benito, M., Lorenzo, M. Exp. Cell Res. (1998) [Pubmed]
  13. B9-serine residue is crucial for insulin actions in glucose metabolism. Liao, Z.Y., Tang, Y.H., Xu, M.H., Feng, Y.M., Zhu, S.Q. Acta Pharmacol. Sin. (2001) [Pubmed]
  14. Insulin increases the association of Akt-2 with Glut4-containing vesicles. Calera, M.R., Martinez, C., Liu, H., Jack, A.K., Birnbaum, M.J., Pilch, P.F. J. Biol. Chem. (1998) [Pubmed]
  15. Discrete structural domains determine differential endoplasmic reticulum to Golgi transit times for glucose transporter isoforms. Hresko, R.C., Murata, H., Marshall, B.A., Mueckler, M. J. Biol. Chem. (1994) [Pubmed]
  16. Transcriptional activation of the glucose transporter GLUT1 in ventricular cardiac myocytes by hypertrophic agonists. Montessuit, C., Thorburn, A. J. Biol. Chem. (1999) [Pubmed]
  17. ATP-sensitive binding of a 70-kDa cytosolic protein to the glucose transporter in rat adipocytes. Liu, H., Xiong, S., Shi, Y., Samuel, S.J., Lachaal, M., Jung, C.Y. J. Biol. Chem. (1995) [Pubmed]
  18. Cellugyrin is a marker for a distinct population of intracellular Glut4-containing vesicles. Kupriyanova, T.A., Kandror, K.V. J. Biol. Chem. (2000) [Pubmed]
  19. Alpha-actinin-4 is selectively required for insulin-induced GLUT4 translocation. Talior-Volodarsky, I., Randhawa, V.K., Zaid, H., Klip, A. J. Biol. Chem. (2008) [Pubmed]
  20. The effects of severe maternal diabetes on glucose transport in the fetal rat. Atkins, V., Flozak, A.S., Ogata, E.S., Simmons, R.A. Endocrinology (1994) [Pubmed]
  21. Insulin resistance in fat cells from obese Zucker rats--evidence for an impaired activation and translocation of protein kinase B and glucose transporter 4. Carvalho, E., Rondinone, C., Smith, U. Mol. Cell. Biochem. (2000) [Pubmed]
  22. Effect of food restriction on the insulin signalling pathway in rat skeletal muscle and adipose tissue. Alonso, A., Fernández, Y., Fernández, R., Ordóñez, P., Moreno, M., Díaz, F., Patterson, A.M., González, C. J. Nutr. Biochem. (2005) [Pubmed]
  23. Regulation of glucose transporters by estradiol in the immature rat uterus. Welch, R.D., Gorski, J. Endocrinology (1999) [Pubmed]
  24. Simultaneous measurement of multiple mRNAs with a single control by quantitative competitive reverse transcriptase-polymerase chain reaction: glucose transporters Glut1 and Glut4. Welch, R.D., Anderson, I., Gorski, J. Anal. Biochem. (1999) [Pubmed]
  25. Expression of Glut-4 and Glut-1 transporters in rat diaphragm muscle. Nie, X., Hida, W., Kikuchi, Y., Kurosawa, H., Tabata, M., Kitamuro, T., Adachi, T., Ohno, I., Shirato, K. Tissue & cell. (2000) [Pubmed]
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