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Book ; Online: AMP-Activated Protein Kinase Signalling

Viollet, Benoit / Neumann, Dietbert

2019

Abstract: Starting from a kinase of interest, AMP-activated protein kinase (AMPK) has gone far beyond an average biomolecule. Being expressed in all mammalian cell types and probably having a counterpart in every eukaryotic cell, AMPK has attracted interest in ... ...

Abstract	Starting from a kinase of interest, AMP-activated protein kinase (AMPK) has gone far beyond an average biomolecule. Being expressed in all mammalian cell types and probably having a counterpart in every eukaryotic cell, AMPK has attracted interest in virtually all areas of biological research. Structural and biophysical insights have greatly contributed to a molecular understanding of this kinase. From good old protein biochemistry to modern approaches, such as systems biology and advanced microscopy, all disciplines have provided important information. Thus, multiple links to cellular events and subcellular localizations have been established. Moreover, the crucial involvement of AMPK in human health and disease has been evidenced. AMPK accordingly has moved from an interesting enzyme to a pharmacological target. However, despite our extensive current knowledge about AMPK, the growing community is busier than ever. This book provides a snapshot of recent and current AMPK research with an emphasis on work providing molecular insight, including but not limited to novel physiological and pathological functions, or regulatory mechanisms. Up-to-date reviews and research articles are included
Keywords	Science (General) ; Biology (General)
Size	1 electronic resource (452 p.)
Publisher	MDPI - Multidisciplinary Digital Publishing Institute
Document type	Book ; Online
Note	eng ; Open Access
HBZ-ID	HT020102470
ISBN	9783038976622 ; 3038976628
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article: Dynamics and differential proliferation of transposable elements during the evolution of the B and A genomes of wheat.

Charles, Mathieu / Belcram, Harry / Just, Jérémy / Huneau, Cécile / Viollet, Agnès / Couloux, Arnaud / Segurens, Béatrice / Carter, Meredith / Huteau, Virginie / Coriton, Olivier / Appels, Rudi / Samain, Sylvie / Chalhoub, Boulos

Genetics

2008 Volume 180, Issue 2, Page(s) 1071–1086

Abstract: ... with all publicly available genomic sequences of wheat, 1.98 Mb of sequence (from 13 BAC clones) of the wheat B ... proliferation in the B and A genomes of wheat. While both genomes show similar rates and relatively ancient ... in the A genome whereas Gypsy retrotransposon proliferation is more recent in the B genome. It was possible ...

Abstract	Transposable elements (TEs) constitute >80% of the wheat genome but their dynamics and contribution to size variation and evolution of wheat genomes (Triticum and Aegilops species) remain unexplored. In this study, 10 genomic regions have been sequenced from wheat chromosome 3B and used to constitute, along with all publicly available genomic sequences of wheat, 1.98 Mb of sequence (from 13 BAC clones) of the wheat B genome and 3.63 Mb of sequence (from 19 BAC clones) of the wheat A genome. Analysis of TE sequence proportions (as percentages), ratios of complete to truncated copies, and estimation of insertion dates of class I retrotransposons showed that specific types of TEs have undergone waves of differential proliferation in the B and A genomes of wheat. While both genomes show similar rates and relatively ancient proliferation periods for the Athila retrotransposons, the Copia retrotransposons proliferated more recently in the A genome whereas Gypsy retrotransposon proliferation is more recent in the B genome. It was possible to estimate for the first time the proliferation periods of the abundant CACTA class II DNA transposons, relative to that of the three main retrotransposon superfamilies. Proliferation of these TEs started prior to and overlapped with that of the Athila retrotransposons in both genomes. However, they also proliferated during the same periods as Gypsy and Copia retrotransposons in the A genome, but not in the B genome. As estimated from their insertion dates and confirmed by PCR-based tracing analysis, the majority of differential proliferation of TEs in B and A genomes of wheat (87 and 83%, respectively), leading to rapid sequence divergence, occurred prior to the allotetraploidization event that brought them together in Triticum turgidum and Triticum aestivum, <0.5 million years ago. More importantly, the allotetraploidization event appears to have neither enhanced nor repressed retrotranspositions. We discuss the apparent proliferation of TEs as resulting from their insertion, removal, and/or combinations of both evolutionary forces.
MeSH term(s)	DNA Transposable Elements/genetics ; Evolution, Molecular ; Genome, Plant ; Molecular Sequence Data ; Triticum/genetics
Chemical Substances	DNA Transposable Elements
Language	English
Publishing date	2008-09-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2167-2
ISSN	1943-2631 ; 0016-6731
ISSN (online)	1943-2631
ISSN	0016-6731
DOI	10.1534/genetics.108.092304
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Article ; Online: Protein kinase CK2 acts as a signal molecule switching between the NDPK-A/AMPK 1 complex and NDPK-B.

Crawford, Russell M / Treharne, Kate J / Arnaud-Dabernat, Sandrine / Daniel, Jean-Yves / Foretz, Marc / Viollet, Benoit / Mehta, Anil

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2007 Volume 21, Issue 12, Page(s) 3398

Language	English
Publishing date	2007-09-25
Publishing country	United States
Document type	Retraction of Publication
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
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Article ; Online: Protein kinase CK2 acts as a signal molecule switching between the NDPK-A/AMPK alpha1 complex and NDPK-B.

Crawford, Russell M / Treharne, Kate J / Arnaud-Dabernat, Sandrine / Daniel, Jean-Yves / Foretz, Marc / Viollet, Benoit / Mehta, Anil

publication RETRACTED

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2007 Volume 21, Issue 1, Page(s) 88–98

Abstract: ... the catalytic subunit of CK2 (CK2alpha) is expelled from the complex and translocates to bind NDPK-B, a closely related ... whether CK2alpha swaps partners between NDPK-A and NDPK-B. This is the first reported linkage between NDPK-A and ... NDPK-B via a phosphorylation pathway and could explain the complex biology of NDPK. This study also ...

Abstract	Previously we elucidated the molecular interaction between the nucleoside diphosphate kinase A (NDPK-A)/AMP-activated protein kinase (AMPK) alpha1 complex, discovering a process we termed "substrate channeling." Here, we investigate the protein-protein interaction of the substrate channeling complex with the pleiotropic protein kinase, CK2 (formerly casein kinase 2). We show that CK2 is part of the NDPK-A/AMPK alpha1 complex under basal (background AMPK activity) conditions, binding directly to each of the complex components independently. We report that when S122 on NDPK-A is phosphorylated by AMPK alpha1 in vivo, (i.e., stimulation of AMPK using either metformin or phenformin) initiating the substrate channeling mechanism, the catalytic subunit of CK2 (CK2alpha) is expelled from the complex and translocates to bind NDPK-B, a closely related but independent isoform of NDPK. Thus, we find that the AMPK-dependent phospho-status of S122 on NDPK-A determines whether CK2alpha swaps partners between NDPK-A and NDPK-B. This is the first reported linkage between NDPK-A and NDPK-B via a phosphorylation pathway and could explain the complex biology of NDPK. This study also offers an explanation as to how CK2alpha exclusion mutations (S120A or S122D of NDPK-A) on NDPK-A might have implications in cancer biology and general cellular energy metabolism.
MeSH term(s)	AMP-Activated Protein Kinases ; Amino Acid Sequence ; Casein Kinase II/chemistry ; Casein Kinase II/metabolism ; Catalytic Domain ; Humans ; Molecular Sequence Data ; Multienzyme Complexes/metabolism ; NM23 Nucleoside Diphosphate Kinases ; Nucleoside-Diphosphate Kinase/metabolism ; Phosphorylation ; Protein Binding ; Protein Transport ; Protein-Serine-Threonine Kinases/metabolism ; Signal Transduction
Chemical Substances	Multienzyme Complexes ; NM23 Nucleoside Diphosphate Kinases ; Casein Kinase II (EC 2.7.11.1) ; PRKAA1 protein, human (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; AMP-Activated Protein Kinases (EC 2.7.11.31) ; Nucleoside-Diphosphate Kinase (EC 2.7.4.6)
Language	English
Publishing date	2007-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Retracted Publication
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.06-6804com
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Article ; Online: Metformin: update on mechanisms of action and repurposing potential.

Foretz, Marc / Guigas, Bruno / Viollet, Benoit

Nature reviews. Endocrinology

2023 Volume 19, Issue 8, Page(s) 460–476

Abstract: Currently, metformin is the first-line medication to treat type 2 diabetes mellitus (T2DM) in most guidelines and is used daily by >200 million patients. Surprisingly, the mechanisms underlying its therapeutic action are complex and are still not fully ... ...

Abstract	Currently, metformin is the first-line medication to treat type 2 diabetes mellitus (T2DM) in most guidelines and is used daily by >200 million patients. Surprisingly, the mechanisms underlying its therapeutic action are complex and are still not fully understood. Early evidence highlighted the liver as the major organ involved in the effect of metformin on reducing blood levels of glucose. However, increasing evidence points towards other sites of action that might also have an important role, including the gastrointestinal tract, the gut microbial communities and the tissue-resident immune cells. At the molecular level, it seems that the mechanisms of action vary depending on the dose of metformin used and duration of treatment. Initial studies have shown that metformin targets hepatic mitochondria; however, the identification of a novel target at low concentrations of metformin at the lysosome surface might reveal a new mechanism of action. Based on the efficacy and safety records in T2DM, attention has been given to the repurposing of metformin as part of adjunct therapy for the treatment of cancer, age-related diseases, inflammatory diseases and COVID-19. In this Review, we highlight the latest advances in our understanding of the mechanisms of action of metformin and discuss potential emerging novel therapeutic uses.
MeSH term(s)	Humans ; Metformin/therapeutic use ; Metformin/pharmacology ; Diabetes Mellitus, Type 2/drug therapy ; Hypoglycemic Agents/pharmacology ; Hypoglycemic Agents/therapeutic use ; COVID-19 ; Glucose
Chemical Substances	Metformin (9100L32L2N) ; Hypoglycemic Agents ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2023-05-02
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2489381-X
ISSN	1759-5037 ; 1759-5029
ISSN (online)	1759-5037
ISSN	1759-5029
DOI	10.1038/s41574-023-00833-4
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Zs.MG 93: Show issues

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Book ; Online: The Energy Sensor AMPK

Viollet, Benoit

Adaptations to Exercise, Nutritional and Hormonal Signals

2019

Abstract: To sustain metabolism, intracellular ATP concentration must be regulated within an appropriate range. This coordination is achieved through the function of the AMP-activated protein kinase (AMPK), a cellular "fuel gauge" that is expressed in essentially ... ...

Abstract	To sustain metabolism, intracellular ATP concentration must be regulated within an appropriate range. This coordination is achieved through the function of the AMP-activated protein kinase (AMPK), a cellular "fuel gauge" that is expressed in essentially all eukaryotic cells as heterotrimeric complexes containing catalytic $\alpha$ subunits and regulatory $\beta$ and $\gamma$ subunits. When cellular energy status has been compromised, AMPK is activated by increases in AMP:ATP or ADP:ATP ratios and acts to restore energy homeostasis by stimulating energy production via catabolic pathways while decreasing non-essential energy-consuming pathways. Although the primary function of AMPK is to regulate energy homeostasis at a cell-autonomous level, in multicellular organisms, the AMPK system has evolved to interact with hormones to regulate energy intake and expenditure at the whole body level. Thus, AMPK functions as a signaling hub, coordinating anabolic and catabolic pathways to balance nutrient supply with energy demand at both the cellular and whole-body levels. AMPK is activated by various metabolic stresses such as ischemia or hypoxia or glucose deprivation and has both acute and long-term effects on metabolic pathways and key cellular functions. In addition, AMPK appears to be a major sensor of energy demand in exercising muscle and acts both as a multitask gatekeeper and an energy regulator in skeletal muscle. Acute activation of AMPK has been shown to promote glucose transport and fatty acid oxidation while suppressing glycogen synthase activity and protein synthesis. Chronic activation of AMPK induces a shift in muscle fiber type composition, reduces markers of muscle degeneration and enhances muscle oxidative capacity potentially by stimulating mitochondrial biogenesis. Furthermore, recent evidence demonstrates that AMPK may not only regulate metabolism during exercise but also in the recovery phase. AMPK acts as a molecular transducer between exercise and insulin signaling and is necessary for the ability of prior contraction/exercise to increase muscle insulin sensitivity. Based on these observations, drugs that activate AMPK might be expected to be useful in the treatment of metabolic disorders and insulin resistance in various conditions.
Keywords	Quantitative Biology - Tissues and Organs
Subject code	571
Publishing date	2019-11-06
Publishing country	us
Document type	Book ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: LRH-1/hB1F and HNF1 synergistically up-regulate hepatitis B virus gene transcription and DNA replication.

Cai, Yan Ning / Zhou, Qing / Kong, Yu Ying / Li, Mei / Viollet, Benoit / Xie, You Hua / Wang, Yuan

Cell research

2003 Volume 13, Issue 6, Page(s) 451–458

Abstract: Enhancer II (ENII) is one of the critical cis-elements in the Hepatitis B Virus (HBV) genome ...

Abstract	Enhancer II (ENII) is one of the critical cis-elements in the Hepatitis B Virus (HBV) genome for the hepatic viral gene transcription and DNA replication. The liver-specific activity of ENII is regulated by multiple liver-enriched transcription factors, including LRH-1/hB1F, HNF1, HNF3b, HNF4 and C/EBP. Knowledge on the interplay of these important factors is still limited. In this study, we demonstrate a functional synergism between the orphan nuclear receptor LRH-1/hB1F and the homeoprotein HNF1 in up-regulating the liver-specific activity of ENII. This synergism is sufficient for initiating the viral gene transcription and DNA replication in non-hepatic cells. We have defined the activation domains in hB1F and HNF1 that contribute to the synergism. We further show that hB1F and HNF1 can interact directly in vitro and have mapped the domains required for this interaction.
MeSH term(s)	Base Sequence ; Binding Sites ; Carcinoma, Hepatocellular ; Catalase/analysis ; DNA Replication ; DNA-Binding Proteins ; Gene Expression Regulation, Viral ; Glutathione Transferase/metabolism ; HeLa Cells ; Hepatitis B virus/genetics ; Hepatitis B virus/physiology ; Hepatocyte Nuclear Factor 1 ; Hepatocyte Nuclear Factor 1-alpha ; Hepatocyte Nuclear Factor 1-beta ; Humans ; Nuclear Proteins ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Receptors, Cytoplasmic and Nuclear ; Recombinant Fusion Proteins/metabolism ; Sequence Deletion ; Trans-Activators/chemistry ; Trans-Activators/metabolism ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcription, Genetic ; Tumor Cells, Cultured ; Virus Replication
Chemical Substances	DNA-Binding Proteins ; HNF1A protein, human ; HNF1B protein, human ; Hepatocyte Nuclear Factor 1-alpha ; NR5A2 protein, human ; Nuclear Proteins ; Receptors, Cytoplasmic and Nuclear ; Recombinant Fusion Proteins ; Trans-Activators ; Transcription Factors ; Hepatocyte Nuclear Factor 1 (126548-29-6) ; Hepatocyte Nuclear Factor 1-beta (138674-15-4) ; Catalase (EC 1.11.1.6) ; Glutathione Transferase (EC 2.5.1.18)
Language	English
Publishing date	2003-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1319303-x
ISSN	1748-7838 ; 1001-0602
ISSN (online)	1748-7838
ISSN	1001-0602
DOI	10.1038/sj.cr.7290187
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Article ; Online: AMP-Activated Protein Kinase Signalling.

Neumann, Dietbert / Viollet, Benoit

International journal of molecular sciences

2019 Volume 20, Issue 3

Abstract: AMP-activated protein kinase (AMPK) regulates energy homeostasis in eukaryotic cells and organisms [ ... ]. ...

Abstract	AMP-activated protein kinase (AMPK) regulates energy homeostasis in eukaryotic cells and organisms [...].
MeSH term(s)	AMP-Activated Protein Kinases/metabolism ; Animals ; Energy Metabolism/physiology ; Homeostasis/physiology ; Humans ; Signal Transduction/physiology
Chemical Substances	AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2019-02-12
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms20030766
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Article: Editorial: AMPK and mTOR Beyond Signaling: Emerging Roles in Transcriptional Regulation.

Audet-Walsh, Étienne / Vernier, Mathieu / Viollet, Benoit

Frontiers in cell and developmental biology

2021 Volume 8, Page(s) 641552

Language	English
Publishing date	2021-01-15
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2020.641552
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Article ; Online: Measurement of AMPK-Induced Inhibition of Lipid Synthesis Flux in Cultured Cells.

Foretz, Marc / Viollet, Benoit

Methods in molecular biology (Clifton, N.J.)

2018 Volume 1732, Page(s) 363–371

Abstract: AMP-activated protein kinase (AMPK) is a master regulator of multiple cellular metabolic pathways, including lipid metabolism. Some of the well-known substrates of AMPK are acetyl-CoA carboxylase (ACC) and 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) ... ...

Abstract	AMP-activated protein kinase (AMPK) is a master regulator of multiple cellular metabolic pathways, including lipid metabolism. Some of the well-known substrates of AMPK are acetyl-CoA carboxylase (ACC) and 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, regulatory enzymes of fatty acid and cholesterol synthesis, respectively. The discovery that both of them are inactivated by AMPK suggested the therapeutic potential of AMPK activation in the treatment of metabolic diseases associated with lipid disorders, such as nonalcoholic fatty liver disease (NAFLD). Here we describe a method to measure lipid synthesis flux in intact cells from the saponifiable (including fatty acids) and non-saponifiable (including sterols) fractions of lipid extracts.
MeSH term(s)	AMP-Activated Protein Kinases/metabolism ; Acetyl-CoA Carboxylase/metabolism ; Animals ; Cell Line ; Cells, Cultured ; Hepatocytes ; Hydroxymethylglutaryl CoA Reductases/metabolism ; Lipids/analysis ; Lipogenesis ; Mice ; Primary Cell Culture
Chemical Substances	Lipids ; Hydroxymethylglutaryl CoA Reductases (EC 1.1.1.-) ; AMP-Activated Protein Kinases (EC 2.7.11.31) ; Acetyl-CoA Carboxylase (EC 6.4.1.2)
Language	English
Publishing date	2018-02-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-7598-3_23
Database	MEDical Literature Analysis and Retrieval System OnLINE

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