AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic and regulatory subunits.

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Standard

AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic and regulatory subunits. / Treebak, Jonas T; Glund, Stephan; Deshmukh, Atul; Klein, Ditte K; Long, Yun Chau; Jensen, Thomas E; Jørgensen, Sebastian B; Viollet, Benoit; Andersson, Leif; Neumann, Dietbert; Wallimann, Theo; Richter, Erik A; Chibalin, Alexander V; Zierath, Juleen R; Wojtaszewski, Jørgen F P.

I: Diabetes, Bind 55, Nr. 7, 2006, s. 2051-8.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Treebak, JT, Glund, S, Deshmukh, A, Klein, DK, Long, YC, Jensen, TE, Jørgensen, SB, Viollet, B, Andersson, L, Neumann, D, Wallimann, T, Richter, EA, Chibalin, AV, Zierath, JR & Wojtaszewski, JFP 2006, 'AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic and regulatory subunits.', Diabetes, bind 55, nr. 7, s. 2051-8. https://doi.org/10.2337/db06-0175

APA

Treebak, J. T., Glund, S., Deshmukh, A., Klein, D. K., Long, Y. C., Jensen, T. E., ... Wojtaszewski, J. F. P. (2006). AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic and regulatory subunits. Diabetes, 55(7), 2051-8. https://doi.org/10.2337/db06-0175

Vancouver

Treebak JT, Glund S, Deshmukh A, Klein DK, Long YC, Jensen TE o.a. AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic and regulatory subunits. Diabetes. 2006;55(7):2051-8. https://doi.org/10.2337/db06-0175

Author

Treebak, Jonas T ; Glund, Stephan ; Deshmukh, Atul ; Klein, Ditte K ; Long, Yun Chau ; Jensen, Thomas E ; Jørgensen, Sebastian B ; Viollet, Benoit ; Andersson, Leif ; Neumann, Dietbert ; Wallimann, Theo ; Richter, Erik A ; Chibalin, Alexander V ; Zierath, Juleen R ; Wojtaszewski, Jørgen F P. / AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic and regulatory subunits. I: Diabetes. 2006 ; Bind 55, Nr. 7. s. 2051-8.

Bibtex

@article{2f0c83b0525511dd8d9f000ea68e967b,
title = "AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic and regulatory subunits.",
abstract = "AMP-activated protein kinase (AMPK) is a heterotrimeric protein that regulates glucose transport mediated by cellular stress or pharmacological agonists such as 5-aminoimidazole-4-carboxamide 1 beta-d-ribonucleoside (AICAR). AS160, a Rab GTPase-activating protein, provides a mechanism linking AMPK signaling to glucose uptake. We show that AICAR increases AMPK, acetyl-CoA carboxylase, and AS160 phosphorylation by insulin-independent mechanisms in isolated skeletal muscle. Recombinant AMPK heterotrimeric complexes (alpha1beta1gamma1 and alpha2beta2gamma1) phosphorylate AS160 in a cell-free assay. In mice deficient in AMPK signaling (alpha2 AMPK knockout [KO], alpha2 AMPK kinase dead [KD], and gamma3 AMPK KO), AICAR effects on AS160 phosphorylation were severely blunted, highlighting that complexes containing alpha2 and gamma3 are necessary for AICAR-stimulated AS160 phosphorylation in intact skeletal muscle. Contraction-mediated AS160 phosphorylation was also impaired in alpha2 AMPK KO and KD but not gamma3 AMPK KO mice. Our results implicate AS160 as a downstream target of AMPK.",
author = "Treebak, {Jonas T} and Stephan Glund and Atul Deshmukh and Klein, {Ditte K} and Long, {Yun Chau} and Jensen, {Thomas E} and J{\o}rgensen, {Sebastian B} and Benoit Viollet and Leif Andersson and Dietbert Neumann and Theo Wallimann and Richter, {Erik A} and Chibalin, {Alexander V} and Zierath, {Juleen R} and Wojtaszewski, {J{\o}rgen F P}",
note = "Keywords: Adenylate Kinase; Aminoimidazole Carboxamide; Animals; Biological Transport; Catalysis; GTPase-Activating Proteins; Glucose; Insulin; Kinetics; Mice; Mice, Knockout; Muscle, Skeletal; Phosphorylation; Protein Subunits; Ribonucleotides",
year = "2006",
doi = "10.2337/db06-0175",
language = "English",
volume = "55",
pages = "2051--8",
journal = "Diabetes",
issn = "0012-1797",
publisher = "American Diabetes Association",
number = "7",

}

RIS

TY - JOUR

T1 - AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic and regulatory subunits.

AU - Treebak, Jonas T

AU - Glund, Stephan

AU - Deshmukh, Atul

AU - Klein, Ditte K

AU - Long, Yun Chau

AU - Jensen, Thomas E

AU - Jørgensen, Sebastian B

AU - Viollet, Benoit

AU - Andersson, Leif

AU - Neumann, Dietbert

AU - Wallimann, Theo

AU - Richter, Erik A

AU - Chibalin, Alexander V

AU - Zierath, Juleen R

AU - Wojtaszewski, Jørgen F P

N1 - Keywords: Adenylate Kinase; Aminoimidazole Carboxamide; Animals; Biological Transport; Catalysis; GTPase-Activating Proteins; Glucose; Insulin; Kinetics; Mice; Mice, Knockout; Muscle, Skeletal; Phosphorylation; Protein Subunits; Ribonucleotides

PY - 2006

Y1 - 2006

N2 - AMP-activated protein kinase (AMPK) is a heterotrimeric protein that regulates glucose transport mediated by cellular stress or pharmacological agonists such as 5-aminoimidazole-4-carboxamide 1 beta-d-ribonucleoside (AICAR). AS160, a Rab GTPase-activating protein, provides a mechanism linking AMPK signaling to glucose uptake. We show that AICAR increases AMPK, acetyl-CoA carboxylase, and AS160 phosphorylation by insulin-independent mechanisms in isolated skeletal muscle. Recombinant AMPK heterotrimeric complexes (alpha1beta1gamma1 and alpha2beta2gamma1) phosphorylate AS160 in a cell-free assay. In mice deficient in AMPK signaling (alpha2 AMPK knockout [KO], alpha2 AMPK kinase dead [KD], and gamma3 AMPK KO), AICAR effects on AS160 phosphorylation were severely blunted, highlighting that complexes containing alpha2 and gamma3 are necessary for AICAR-stimulated AS160 phosphorylation in intact skeletal muscle. Contraction-mediated AS160 phosphorylation was also impaired in alpha2 AMPK KO and KD but not gamma3 AMPK KO mice. Our results implicate AS160 as a downstream target of AMPK.

AB - AMP-activated protein kinase (AMPK) is a heterotrimeric protein that regulates glucose transport mediated by cellular stress or pharmacological agonists such as 5-aminoimidazole-4-carboxamide 1 beta-d-ribonucleoside (AICAR). AS160, a Rab GTPase-activating protein, provides a mechanism linking AMPK signaling to glucose uptake. We show that AICAR increases AMPK, acetyl-CoA carboxylase, and AS160 phosphorylation by insulin-independent mechanisms in isolated skeletal muscle. Recombinant AMPK heterotrimeric complexes (alpha1beta1gamma1 and alpha2beta2gamma1) phosphorylate AS160 in a cell-free assay. In mice deficient in AMPK signaling (alpha2 AMPK knockout [KO], alpha2 AMPK kinase dead [KD], and gamma3 AMPK KO), AICAR effects on AS160 phosphorylation were severely blunted, highlighting that complexes containing alpha2 and gamma3 are necessary for AICAR-stimulated AS160 phosphorylation in intact skeletal muscle. Contraction-mediated AS160 phosphorylation was also impaired in alpha2 AMPK KO and KD but not gamma3 AMPK KO mice. Our results implicate AS160 as a downstream target of AMPK.

U2 - 10.2337/db06-0175

DO - 10.2337/db06-0175

M3 - Journal article

C2 - 16804075

VL - 55

SP - 2051

EP - 2058

JO - Diabetes

JF - Diabetes

SN - 0012-1797

IS - 7

ER -

ID: 5015872