A noncanonical, GSK3-independent pathway controls postprandial hepatic glycogen deposition

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A noncanonical, GSK3-independent pathway controls postprandial hepatic glycogen deposition. / Wan, Min; Leavens, Karla F.; Hunter, Roger W.; Koren, Shlomit; Von Wilamowitz-Moellendorff, Alexander; Lu, Mingjian; Satapati, Santhosh; Chu, Qingwei; Sakamoto, Kei; Burgess, Shawn C.; Birnbaum, Morris J.

In: Cell Metabolism, Vol. 18, No. 1, 02.07.2013, p. 99-105.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Wan, M, Leavens, KF, Hunter, RW, Koren, S, Von Wilamowitz-Moellendorff, A, Lu, M, Satapati, S, Chu, Q, Sakamoto, K, Burgess, SC & Birnbaum, MJ 2013, 'A noncanonical, GSK3-independent pathway controls postprandial hepatic glycogen deposition', Cell Metabolism, vol. 18, no. 1, pp. 99-105. https://doi.org/10.1016/j.cmet.2013.06.001

APA

Wan, M., Leavens, K. F., Hunter, R. W., Koren, S., Von Wilamowitz-Moellendorff, A., Lu, M., Satapati, S., Chu, Q., Sakamoto, K., Burgess, S. C., & Birnbaum, M. J. (2013). A noncanonical, GSK3-independent pathway controls postprandial hepatic glycogen deposition. Cell Metabolism, 18(1), 99-105. https://doi.org/10.1016/j.cmet.2013.06.001

Vancouver

Wan M, Leavens KF, Hunter RW, Koren S, Von Wilamowitz-Moellendorff A, Lu M et al. A noncanonical, GSK3-independent pathway controls postprandial hepatic glycogen deposition. Cell Metabolism. 2013 Jul 2;18(1):99-105. https://doi.org/10.1016/j.cmet.2013.06.001

Author

Wan, Min ; Leavens, Karla F. ; Hunter, Roger W. ; Koren, Shlomit ; Von Wilamowitz-Moellendorff, Alexander ; Lu, Mingjian ; Satapati, Santhosh ; Chu, Qingwei ; Sakamoto, Kei ; Burgess, Shawn C. ; Birnbaum, Morris J. / A noncanonical, GSK3-independent pathway controls postprandial hepatic glycogen deposition. In: Cell Metabolism. 2013 ; Vol. 18, No. 1. pp. 99-105.

Bibtex

@article{9c84c11300b3468182cb819fac759850,
title = "A noncanonical, GSK3-independent pathway controls postprandial hepatic glycogen deposition",
abstract = "Insulin rapidly suppresses hepatic glucose production and slowly decreases expression of genes encoding gluconeogenic proteins. In this study, we show that an immediate effect of insulin is to redirect newly synthesized glucose-6-phosphate to glycogen without changing the rate of gluconeogenesis. This process requires hepatic Akt2, as revealed by blunted insulin-mediated suppression of glycogenolysis in the perfused mouse liver, elevated hepatic glucose production during a euglycemic-hyperinsulinemic clamp, or diminished glycogen accumulation during clamp or refeeding in mice without hepatic Akt2. Surprisingly, the absence of Akt2 disrupted glycogen metabolism independent of GSK3α and GSK3β phosphorylation, which is thought to be an essential step in the pathway by which insulin regulates glycogen synthesis through Akt. These data show that (1) the immediate action of insulin to suppress hepatic glucose production functions via an Akt2-dependent redirection of glucose-6-phosphate to glycogen, and (2) insulin increases glucose phosphorylation and conversion to glycogen independent of GSK3.",
author = "Min Wan and Leavens, {Karla F.} and Hunter, {Roger W.} and Shlomit Koren and {Von Wilamowitz-Moellendorff}, Alexander and Mingjian Lu and Santhosh Satapati and Qingwei Chu and Kei Sakamoto and Burgess, {Shawn C.} and Birnbaum, {Morris J.}",
year = "2013",
month = jul,
day = "2",
doi = "10.1016/j.cmet.2013.06.001",
language = "English",
volume = "18",
pages = "99--105",
journal = "Cell Metabolism",
issn = "1550-4131",
publisher = "Cell Press",
number = "1",

}

RIS

TY - JOUR

T1 - A noncanonical, GSK3-independent pathway controls postprandial hepatic glycogen deposition

AU - Wan, Min

AU - Leavens, Karla F.

AU - Hunter, Roger W.

AU - Koren, Shlomit

AU - Von Wilamowitz-Moellendorff, Alexander

AU - Lu, Mingjian

AU - Satapati, Santhosh

AU - Chu, Qingwei

AU - Sakamoto, Kei

AU - Burgess, Shawn C.

AU - Birnbaum, Morris J.

PY - 2013/7/2

Y1 - 2013/7/2

N2 - Insulin rapidly suppresses hepatic glucose production and slowly decreases expression of genes encoding gluconeogenic proteins. In this study, we show that an immediate effect of insulin is to redirect newly synthesized glucose-6-phosphate to glycogen without changing the rate of gluconeogenesis. This process requires hepatic Akt2, as revealed by blunted insulin-mediated suppression of glycogenolysis in the perfused mouse liver, elevated hepatic glucose production during a euglycemic-hyperinsulinemic clamp, or diminished glycogen accumulation during clamp or refeeding in mice without hepatic Akt2. Surprisingly, the absence of Akt2 disrupted glycogen metabolism independent of GSK3α and GSK3β phosphorylation, which is thought to be an essential step in the pathway by which insulin regulates glycogen synthesis through Akt. These data show that (1) the immediate action of insulin to suppress hepatic glucose production functions via an Akt2-dependent redirection of glucose-6-phosphate to glycogen, and (2) insulin increases glucose phosphorylation and conversion to glycogen independent of GSK3.

AB - Insulin rapidly suppresses hepatic glucose production and slowly decreases expression of genes encoding gluconeogenic proteins. In this study, we show that an immediate effect of insulin is to redirect newly synthesized glucose-6-phosphate to glycogen without changing the rate of gluconeogenesis. This process requires hepatic Akt2, as revealed by blunted insulin-mediated suppression of glycogenolysis in the perfused mouse liver, elevated hepatic glucose production during a euglycemic-hyperinsulinemic clamp, or diminished glycogen accumulation during clamp or refeeding in mice without hepatic Akt2. Surprisingly, the absence of Akt2 disrupted glycogen metabolism independent of GSK3α and GSK3β phosphorylation, which is thought to be an essential step in the pathway by which insulin regulates glycogen synthesis through Akt. These data show that (1) the immediate action of insulin to suppress hepatic glucose production functions via an Akt2-dependent redirection of glucose-6-phosphate to glycogen, and (2) insulin increases glucose phosphorylation and conversion to glycogen independent of GSK3.

UR - http://www.scopus.com/inward/record.url?scp=84879857725&partnerID=8YFLogxK

U2 - 10.1016/j.cmet.2013.06.001

DO - 10.1016/j.cmet.2013.06.001

M3 - Journal article

C2 - 23823480

AN - SCOPUS:84879857725

VL - 18

SP - 99

EP - 105

JO - Cell Metabolism

JF - Cell Metabolism

SN - 1550-4131

IS - 1

ER -

ID: 239565800