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AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase

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AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase. / Bultot, Laurent; Guigas, Bruno; Von Wilamowitz-Moellendorff, Alexander; Maisin, Liliane; Vertommen, Didier; Hussain, Nusrat; Beullens, Monique; Guinovart, Joan J.; Foretz, Marc; Viollet, Benoit; Sakamoto, Kei; Hue, Louis; Rider, Mark H.

In: Biochemical Journal, Vol. 443, 01.04.2012, p. 193-203.

Research output: Contribution to journalArticle

Harvard

Bultot, L, Guigas, B, Von Wilamowitz-Moellendorff, A, Maisin, L, Vertommen, D, Hussain, N, Beullens, M, Guinovart, JJ, Foretz, M, Viollet, B, Sakamoto, K, Hue, L & Rider, MH 2012, 'AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase' Biochemical Journal, vol 443, pp. 193-203.

APA

Bultot, L., Guigas, B., Von Wilamowitz-Moellendorff, A., Maisin, L., Vertommen, D., Hussain, N., Beullens, M., Guinovart, J. J., Foretz, M., Viollet, B., Sakamoto, K., Hue, L., & Rider, M. H. (2012). AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase. Biochemical Journal, 443, 193-203doi: 10.1042/BJ20112026

Vancouver

Bultot L, Guigas B, Von Wilamowitz-Moellendorff A, Maisin L, Vertommen D, Hussain N et al. AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase. Biochemical Journal. 2012 Apr 1;443:193-203.

Author

Bultot, Laurent; Guigas, Bruno; Von Wilamowitz-Moellendorff, Alexander; Maisin, Liliane; Vertommen, Didier; Hussain, Nusrat; Beullens, Monique; Guinovart, Joan J.; Foretz, Marc; Viollet, Benoit; Sakamoto, Kei; Hue, Louis; Rider, Mark H. / AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase.

In: Biochemical Journal, Vol. 443, 01.04.2012, p. 193-203.

Research output: Contribution to journalArticle

Bibtex - Download

@article{b213a05e38de4ee69a26dcbc3c230c98,
title = "AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase",
author = "Laurent Bultot and Bruno Guigas and {Von Wilamowitz-Moellendorff}, Alexander and Liliane Maisin and Didier Vertommen and Nusrat Hussain and Monique Beullens and Guinovart, {Joan J.} and Marc Foretz and Benoit Viollet and Kei Sakamoto and Louis Hue and Rider, {Mark H.}",
year = "2012",
volume = "443",
pages = "193--203",
journal = "Biochemical Journal",
issn = "0264-6021",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase

A1 - Bultot,Laurent

A1 - Guigas,Bruno

A1 - Von Wilamowitz-Moellendorff,Alexander

A1 - Maisin,Liliane

A1 - Vertommen,Didier

A1 - Hussain,Nusrat

A1 - Beullens,Monique

A1 - Guinovart,Joan J.

A1 - Foretz,Marc

A1 - Viollet,Benoit

A1 - Sakamoto,Kei

A1 - Hue,Louis

A1 - Rider,Mark H.

AU - Bultot,Laurent

AU - Guigas,Bruno

AU - Von Wilamowitz-Moellendorff,Alexander

AU - Maisin,Liliane

AU - Vertommen,Didier

AU - Hussain,Nusrat

AU - Beullens,Monique

AU - Guinovart,Joan J.

AU - Foretz,Marc

AU - Viollet,Benoit

AU - Sakamoto,Kei

AU - Hue,Louis

AU - Rider,Mark H.

PY - 2012/4/1

Y1 - 2012/4/1

N2 - <p>Recombinant muscle GYS1 (glycogen synthase 1) and recombinant liver GYS2 were phosphorylated by recombinant AMPK (AMP-activated protein kinase) in a time-dependent manner and to a similar stoichiometry. The phosphorylation site in GYS2 was identified as Ser(7), which lies in a favourable consensus for phosphorylation by AMPK. Phosphorylation of GYS1 or GYS2 by AMPK led to enzyme inactivation by decreasing the affinity for both UDP-Glc (UDP-glucose) [assayed in the absence of Glc-6-P (glucose-6-phosphate)] and Glc-6-P (assayed at low UDP-Glc concentrations). Incubation of freshly isolated rat hepatocytes with the pharmacological AMPK activators AICA riboside (5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside) or A769662 led to persistent GYS inactivation and Ser(7) phosphorylation, whereas inactivation by glucagon treatment was transient. In hepatocytes from mice harbouring a liver-specific deletion of the AMPK catalytic alpha 1/alpha 2 subunits, GYS2 inactivation by AICA riboside and A769662 was blunted, whereas inactivation by glucagon was unaffected. The results suggest that GYS inactivation by AMPK activators in hepatocytes is due to GYS2 Ser(7) phosphorylation.</p>

AB - <p>Recombinant muscle GYS1 (glycogen synthase 1) and recombinant liver GYS2 were phosphorylated by recombinant AMPK (AMP-activated protein kinase) in a time-dependent manner and to a similar stoichiometry. The phosphorylation site in GYS2 was identified as Ser(7), which lies in a favourable consensus for phosphorylation by AMPK. Phosphorylation of GYS1 or GYS2 by AMPK led to enzyme inactivation by decreasing the affinity for both UDP-Glc (UDP-glucose) [assayed in the absence of Glc-6-P (glucose-6-phosphate)] and Glc-6-P (assayed at low UDP-Glc concentrations). Incubation of freshly isolated rat hepatocytes with the pharmacological AMPK activators AICA riboside (5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside) or A769662 led to persistent GYS inactivation and Ser(7) phosphorylation, whereas inactivation by glucagon treatment was transient. In hepatocytes from mice harbouring a liver-specific deletion of the AMPK catalytic alpha 1/alpha 2 subunits, GYS2 inactivation by AICA riboside and A769662 was blunted, whereas inactivation by glucagon was unaffected. The results suggest that GYS inactivation by AMPK activators in hepatocytes is due to GYS2 Ser(7) phosphorylation.</p>

U2 - 10.1042/BJ20112026

DO - 10.1042/BJ20112026

M1 - Article

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

VL - 443

SP - 193

EP - 203

ER -

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