Publication

Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes

Cormont, M., Bortoluzzi, M. N., Gautier, N., Mari, M., van Obberghen, E. & Le Marchand-Brustel, Y., Dec-1996, In : Molecular and Cellular Biology. 16, 12, p. 6879-6886 8 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Cormont, M., Bortoluzzi, M. N., Gautier, N., Mari, M., van Obberghen, E., & Le Marchand-Brustel, Y. (1996). Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes. Molecular and Cellular Biology, 16(12), 6879-6886. https://doi.org/10.1128/MCB.16.12.6879

Author

Cormont, M ; Bortoluzzi, M N ; Gautier, N ; Mari, M ; van Obberghen, E ; Le Marchand-Brustel, Y. / Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes. In: Molecular and Cellular Biology. 1996 ; Vol. 16, No. 12. pp. 6879-6886.

Harvard

Cormont, M, Bortoluzzi, MN, Gautier, N, Mari, M, van Obberghen, E & Le Marchand-Brustel, Y 1996, 'Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes', Molecular and Cellular Biology, vol. 16, no. 12, pp. 6879-6886. https://doi.org/10.1128/MCB.16.12.6879

Standard

Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes. / Cormont, M; Bortoluzzi, M N; Gautier, N; Mari, M; van Obberghen, E; Le Marchand-Brustel, Y.

In: Molecular and Cellular Biology, Vol. 16, No. 12, 12.1996, p. 6879-6886.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Cormont M, Bortoluzzi MN, Gautier N, Mari M, van Obberghen E, Le Marchand-Brustel Y. Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes. Molecular and Cellular Biology. 1996 Dec;16(12):6879-6886. https://doi.org/10.1128/MCB.16.12.6879


BibTeX

@article{558f750a27f64f92af1ff4eea470f5d2,
title = "Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes",
abstract = "A role for Rab4 in the translocation of the glucose transporter Glut4 induced by insulin has been recently proposed. To study more directly the role of this small GTPase, freshly isolated adipocytes were transiently transfected with the cDNAs of both an epitope-tagged Glut4-myc and Rab4, a system which allows direct measurement of the concentration of Glut4 molecules at the cell surface. When cells were cotransfected with Glut4-myc and Rab4, the concentration of Glut4-myc at the cell surface decreased in parallel with the increased expression of Rab4, suggesting that Rab4 participates in the intracellular retention of Glut4. In parallel, the amount of Rab4 associated with the Glut4-containing vesicles increased. When Rab4 was moderately overexpressed, the number of Glut4-myc molecules recruited to the cell surface in response to insulin was similar to that observed in mock-transfected cells, and thus the insulin efficiency was increased. When Rab4 was expressed at a higher level, the amount of Glut4-myc present at the cell surface in response to insulin decreased. Since the overexpressed protein was predominantly cytosolic, this suggests that the cytosolic Rab4 might complex some factor(s) necessary for insulin action. This hypothesis was strengthened by the fact that Rab4 deltaCT, a Rab4 mutant lacking the geranylgeranylation sites, inhibited insulin-induced recruitement of Glut4-myc to the cell surface, even when moderately overexpressed. Rab3D was without effect on Glut4-myc subcellular distribution in basal or insulin-stimulated conditions. While two mutated proteins unable to bind GTP did not decrease the number of Glut4-myc molecules in basal or insulin-stimulated conditions at the plasma membrane, the behavior of a mutated Rab4 protein without GTPase activity was similar to that of the wild-type Rab4 protein, indicating that GTP binding but not its hydrolysis was required for the observed effects. Altogether, our results suggest that Rab4, but not Rab3D, participates in the molecular mechanism involved in the subcellular distribution of the Glut4 molecules both in basal and in insulin-stimulated conditions in adipocytes.",
keywords = "Adipocytes, Animals, Cells, Cultured, GTP-Binding Proteins, Gene Expression Regulation, Gene Transfer Techniques, Glucose Transporter Type 4, Male, Monosaccharide Transport Proteins, Muscle Proteins, Rats, Rats, Wistar, rab4 GTP-Binding Proteins, Journal Article, Research Support, Non-U.S. Gov't",
author = "M Cormont and Bortoluzzi, {M N} and N Gautier and M Mari and {van Obberghen}, E and {Le Marchand-Brustel}, Y",
year = "1996",
month = "12",
doi = "10.1128/MCB.16.12.6879",
language = "English",
volume = "16",
pages = "6879--6886",
journal = "Molecular and Cellular Biology",
issn = "0270-7306",
publisher = "AMER SOC MICROBIOLOGY",
number = "12",

}

RIS

TY - JOUR

T1 - Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes

AU - Cormont, M

AU - Bortoluzzi, M N

AU - Gautier, N

AU - Mari, M

AU - van Obberghen, E

AU - Le Marchand-Brustel, Y

PY - 1996/12

Y1 - 1996/12

N2 - A role for Rab4 in the translocation of the glucose transporter Glut4 induced by insulin has been recently proposed. To study more directly the role of this small GTPase, freshly isolated adipocytes were transiently transfected with the cDNAs of both an epitope-tagged Glut4-myc and Rab4, a system which allows direct measurement of the concentration of Glut4 molecules at the cell surface. When cells were cotransfected with Glut4-myc and Rab4, the concentration of Glut4-myc at the cell surface decreased in parallel with the increased expression of Rab4, suggesting that Rab4 participates in the intracellular retention of Glut4. In parallel, the amount of Rab4 associated with the Glut4-containing vesicles increased. When Rab4 was moderately overexpressed, the number of Glut4-myc molecules recruited to the cell surface in response to insulin was similar to that observed in mock-transfected cells, and thus the insulin efficiency was increased. When Rab4 was expressed at a higher level, the amount of Glut4-myc present at the cell surface in response to insulin decreased. Since the overexpressed protein was predominantly cytosolic, this suggests that the cytosolic Rab4 might complex some factor(s) necessary for insulin action. This hypothesis was strengthened by the fact that Rab4 deltaCT, a Rab4 mutant lacking the geranylgeranylation sites, inhibited insulin-induced recruitement of Glut4-myc to the cell surface, even when moderately overexpressed. Rab3D was without effect on Glut4-myc subcellular distribution in basal or insulin-stimulated conditions. While two mutated proteins unable to bind GTP did not decrease the number of Glut4-myc molecules in basal or insulin-stimulated conditions at the plasma membrane, the behavior of a mutated Rab4 protein without GTPase activity was similar to that of the wild-type Rab4 protein, indicating that GTP binding but not its hydrolysis was required for the observed effects. Altogether, our results suggest that Rab4, but not Rab3D, participates in the molecular mechanism involved in the subcellular distribution of the Glut4 molecules both in basal and in insulin-stimulated conditions in adipocytes.

AB - A role for Rab4 in the translocation of the glucose transporter Glut4 induced by insulin has been recently proposed. To study more directly the role of this small GTPase, freshly isolated adipocytes were transiently transfected with the cDNAs of both an epitope-tagged Glut4-myc and Rab4, a system which allows direct measurement of the concentration of Glut4 molecules at the cell surface. When cells were cotransfected with Glut4-myc and Rab4, the concentration of Glut4-myc at the cell surface decreased in parallel with the increased expression of Rab4, suggesting that Rab4 participates in the intracellular retention of Glut4. In parallel, the amount of Rab4 associated with the Glut4-containing vesicles increased. When Rab4 was moderately overexpressed, the number of Glut4-myc molecules recruited to the cell surface in response to insulin was similar to that observed in mock-transfected cells, and thus the insulin efficiency was increased. When Rab4 was expressed at a higher level, the amount of Glut4-myc present at the cell surface in response to insulin decreased. Since the overexpressed protein was predominantly cytosolic, this suggests that the cytosolic Rab4 might complex some factor(s) necessary for insulin action. This hypothesis was strengthened by the fact that Rab4 deltaCT, a Rab4 mutant lacking the geranylgeranylation sites, inhibited insulin-induced recruitement of Glut4-myc to the cell surface, even when moderately overexpressed. Rab3D was without effect on Glut4-myc subcellular distribution in basal or insulin-stimulated conditions. While two mutated proteins unable to bind GTP did not decrease the number of Glut4-myc molecules in basal or insulin-stimulated conditions at the plasma membrane, the behavior of a mutated Rab4 protein without GTPase activity was similar to that of the wild-type Rab4 protein, indicating that GTP binding but not its hydrolysis was required for the observed effects. Altogether, our results suggest that Rab4, but not Rab3D, participates in the molecular mechanism involved in the subcellular distribution of the Glut4 molecules both in basal and in insulin-stimulated conditions in adipocytes.

KW - Adipocytes

KW - Animals

KW - Cells, Cultured

KW - GTP-Binding Proteins

KW - Gene Expression Regulation

KW - Gene Transfer Techniques

KW - Glucose Transporter Type 4

KW - Male

KW - Monosaccharide Transport Proteins

KW - Muscle Proteins

KW - Rats

KW - Rats, Wistar

KW - rab4 GTP-Binding Proteins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1128/MCB.16.12.6879

DO - 10.1128/MCB.16.12.6879

M3 - Article

VL - 16

SP - 6879

EP - 6886

JO - Molecular and Cellular Biology

JF - Molecular and Cellular Biology

SN - 0270-7306

IS - 12

ER -

ID: 54167739