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Article ; Online: Effect of different γ-subunit isoforms on the regulation of AMPK.

Willows, Robin / Navaratnam, Naveenan / Lima, Ana / Read, Jon / Carling, David

2017 Volume 474, Issue 10, Page(s) 1741–1754

Abstract: AMP-activated protein kinase (AMPK) plays a key role in integrating metabolic pathways in response to energy demand. AMPK activation results in a wide range of downstream responses, many of which are associated with improved metabolic outcome, making ... ...

Abstract	AMP-activated protein kinase (AMPK) plays a key role in integrating metabolic pathways in response to energy demand. AMPK activation results in a wide range of downstream responses, many of which are associated with improved metabolic outcome, making AMPK an attractive target for the treatment of metabolic diseases. AMPK is a heterotrimeric complex consisting of a catalytic subunit (α) and two regulatory subunits (β and γ). The γ-subunit harbours the nucleotide-binding sites and plays an important role in AMPK regulation in response to cellular energy levels. In mammals, there are three isoforms of the γ-subunit and these respond differently to regulation by nucleotides, but there is limited information regarding their role in activation by small molecules. Here, we determined the effect of different γ-isoforms on AMPK by a direct activator, 991. In cells, 991 led to a greater activation of γ2-containing AMPK complexes compared with either γ1 or γ3. This effect was dependent on the long N-terminal region of the γ2-isoform. We were able to rule out an effect of Ser
MeSH term(s)	AMP-Activated Protein Kinases/antagonists & inhibitors ; AMP-Activated Protein Kinases/chemistry ; AMP-Activated Protein Kinases/genetics ; AMP-Activated Protein Kinases/metabolism ; Allosteric Regulation/drug effects ; Amino Acid Substitution ; Aminopyridines/pharmacology ; Benzimidazoles/pharmacology ; Benzoates/pharmacology ; Binding Sites ; CRISPR-Cas Systems ; Enzyme Activation/drug effects ; Enzyme Activators/pharmacology ; HEK293 Cells ; Humans ; Indoles/pharmacology ; Isoenzymes/antagonists & inhibitors ; Isoenzymes/chemistry ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Ligands ; Mutation ; Phosphorylation/drug effects ; Protein Processing, Post-Translational/drug effects ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Threonine/metabolism
Chemical Substances	5-((6-chloro-5-(1-methylindol-5-yl)-1H-benzimidazol-2-yl)oxy)-2-methylbenzoic acid ; Aminopyridines ; Benzimidazoles ; Benzoates ; Enzyme Activators ; Indoles ; Isoenzymes ; Ligands ; PF-249 ; Recombinant Proteins ; Threonine (2ZD004190S) ; PRKAG1 protein, human (EC 2.7.11.1) ; PRKAG2 protein, human (EC 2.7.11.1) ; PRKAG3 protein, human (EC 2.7.11.1) ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2017-05-09
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20170046
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Imaging of Metabolic Status in 3D Cultures with an Improved AMPK FRET Biosensor for FLIM.

Chennell, George / Willows, Robin J W / Warren, Sean C / Carling, David / French, Paul M W / Dunsby, Chris / Sardini, Alessandro

Sensors (Basel, Switzerland)

2016 Volume 16, Issue 8

Abstract: We describe an approach to non-invasively map spatiotemporal biochemical and physiological changes in 3D cell culture using Forster Resonance Energy Transfer (FRET) biosensors expressed in tumour spheroids. In particular, we present an improved Adenosine ...

Abstract	We describe an approach to non-invasively map spatiotemporal biochemical and physiological changes in 3D cell culture using Forster Resonance Energy Transfer (FRET) biosensors expressed in tumour spheroids. In particular, we present an improved Adenosine Monophosphate (AMP) Activated Protein Kinase (AMPK) FRET biosensor, mTurquoise2 AMPK Activity Reporter (T2AMPKAR), for fluorescence lifetime imaging (FLIM) readouts that we have evaluated in 2D and 3D cultures. Our results in 2D cell culture indicate that replacing the FRET donor, enhanced Cyan Fluorescent Protein (ECFP), in the original FRET biosensor, AMPK activity reporter (AMPKAR), with mTurquoise2 (mTq2FP), increases the dynamic range of the response to activation of AMPK, as demonstrated using the direct AMPK activator, 991. We demonstrated 3D FLIM of this T2AMPKAR FRET biosensor expressed in tumour spheroids using two-photon excitation.
MeSH term(s)	AMP-Activated Protein Kinase Kinases ; Biosensing Techniques/methods ; Cell Culture Techniques ; Fluorescence Resonance Energy Transfer/methods ; Green Fluorescent Proteins/chemistry ; Humans ; Molecular Imaging/methods ; Optical Imaging/methods ; Protein Kinases/isolation & purification ; Spheroids, Cellular/cytology
Chemical Substances	enhanced cyan fluorescent protein ; Green Fluorescent Proteins (147336-22-9) ; Protein Kinases (EC 2.7.-) ; AMP-Activated Protein Kinase Kinases (EC 2.7.11.3)
Language	English
Publishing date	2016-08-19
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2052857-7
ISSN	1424-8220 ; 1424-8220
ISSN (online)	1424-8220
ISSN	1424-8220
DOI	10.3390/s16081312
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Mitochondria-derived ROS activate AMP-activated protein kinase (AMPK) indirectly.

Hinchy, Elizabeth C / Gruszczyk, Anja V / Willows, Robin / Navaratnam, Naveenan / Hall, Andrew R / Bates, Georgina / Bright, Thomas P / Krieg, Thomas / Carling, David / Murphy, Michael P

The Journal of biological chemistry

2018 Volume 293, Issue 44, Page(s) 17208–17217

Abstract: Mitochondrial reactive oxygen species (ROS) production is a tightly regulated redox signal that transmits information from the organelle to the cell. Other mitochondrial signals, such as ATP, are sensed by enzymes, including the key metabolic sensor and ... ...

Abstract	Mitochondrial reactive oxygen species (ROS) production is a tightly regulated redox signal that transmits information from the organelle to the cell. Other mitochondrial signals, such as ATP, are sensed by enzymes, including the key metabolic sensor and regulator, AMP-activated protein kinase (AMPK). AMPK responds to the cellular ATP/AMP and ATP/ADP ratios by matching mitochondrial ATP production to demand. Previous reports proposed that AMPK activity also responds to ROS, by ROS acting on redox-sensitive cysteine residues (Cys-299/Cys-304) on the AMPK α subunit. This suggests an appealing model in which mitochondria fine-tune AMPK activity by both adenine nucleotide-dependent mechanisms and by redox signals. Here we assessed whether physiological levels of ROS directly alter AMPK activity. To this end we added exogenous hydrogen peroxide (H
MeSH term(s)	AMP-Activated Protein Kinases/genetics ; AMP-Activated Protein Kinases/metabolism ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Cell Line ; Enzyme Activation ; Humans ; Hydrogen Peroxide/metabolism ; Mice ; Mitochondria/genetics ; Mitochondria/metabolism ; Muscle Fibers, Skeletal/enzymology ; Muscle Fibers, Skeletal/metabolism ; Oxidation-Reduction ; Reactive Oxygen Species/metabolism
Chemical Substances	Reactive Oxygen Species ; Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE) ; Hydrogen Peroxide (BBX060AN9V) ; PRKAA1 protein, human (EC 2.7.11.1) ; PRKAB1 protein, human (EC 2.7.11.1) ; PRKAG1 protein, human (EC 2.7.11.1) ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2018-09-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA118.002579
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Imaging of Metabolic Status in 3D Cultures with an Improved AMPK FRET Biosensor for FLIM

George Chennell / Robin J. W. Willows / Sean C. Warren / David Carling / Paul M. W. French / Chris Dunsby / Alessandro Sardini

Sensors, Vol 16, Iss 8, p

2016 Volume 1312

Abstract	We describe an approach to non-invasively map spatiotemporal biochemical and physiological changes in 3D cell culture using Forster Resonance Energy Transfer (FRET) biosensors expressed in tumour spheroids. In particular, we present an improved Adenosine Monophosphate (AMP) Activated Protein Kinase (AMPK) FRET biosensor, mTurquoise2 AMPK Activity Reporter (T2AMPKAR), for fluorescence lifetime imaging (FLIM) readouts that we have evaluated in 2D and 3D cultures. Our results in 2D cell culture indicate that replacing the FRET donor, enhanced Cyan Fluorescent Protein (ECFP), in the original FRET biosensor, AMPK activity reporter (AMPKAR), with mTurquoise2 (mTq2FP), increases the dynamic range of the response to activation of AMPK, as demonstrated using the direct AMPK activator, 991. We demonstrated 3D FLIM of this T2AMPKAR FRET biosensor expressed in tumour spheroids using two-photon excitation.
Keywords	FRET ; FLIM ; AMPK ; spheroid ; 2-photon ; biosensor ; TCSPC ; 3D culture ; Technology (General) ; T1-995 ; Technology ; T ; Analytical chemistry ; QD71-142 ; Chemistry ; QD1-999 ; Science ; Q ; Chemical technology ; TP1-1185
Language	English
Publishing date	2016-08-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Phosphorylation of AMPK by upstream kinases is required for activity in mammalian cells.

Willows, Robin / Sanders, Matthew J / Xiao, Bing / Patel, Bhakti R / Martin, Stephen R / Read, Jon / Wilson, Jon R / Hubbard, Julia / Gamblin, Steven J / Carling, David

The Biochemical journal

2017 Volume 474, Issue 17, Page(s) 3059–3073

Abstract: AMP-activated protein kinase (AMPK) plays a major role in regulating metabolism and has attracted significant attention as a therapeutic target for treating metabolic disorders. AMPK activity is stimulated more than 100-fold by phosphorylation of ... ...

Abstract	AMP-activated protein kinase (AMPK) plays a major role in regulating metabolism and has attracted significant attention as a therapeutic target for treating metabolic disorders. AMPK activity is stimulated more than 100-fold by phosphorylation of threonine 172 (Thr
MeSH term(s)	A549 Cells ; AMP-Activated Protein Kinase Kinases ; AMP-Activated Protein Kinases/genetics ; AMP-Activated Protein Kinases/metabolism ; Biphenyl Compounds ; Calcium-Calmodulin-Dependent Protein Kinase Kinase/genetics ; Calcium-Calmodulin-Dependent Protein Kinase Kinase/metabolism ; Enzyme Activation/drug effects ; Enzyme Activation/genetics ; HEK293 Cells ; Humans ; Phosphorylation/drug effects ; Phosphorylation/genetics ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Pyrones/pharmacology ; Thiophenes/pharmacology
Chemical Substances	Biphenyl Compounds ; Pyrones ; Thiophenes ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; STK11 protein, human (EC 2.7.11.1) ; Calcium-Calmodulin-Dependent Protein Kinase Kinase (EC 2.7.11.17) ; AMP-Activated Protein Kinase Kinases (EC 2.7.11.3) ; AMP-Activated Protein Kinases (EC 2.7.11.31) ; 4-hydroxy-3-(4-(2-hydroxyphenyl)phenyl)-6-oxo-7H-thieno(2,3-b)pyridine-5-carbonitrile (P68477CD2C)
Language	English
Publishing date	2017-08-22
Publishing country	England
Document type	Journal Article
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20170458
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Article: Soil biota in a megadiverse country: Current knowledge and future research directions in South Africa

Janion-Scheepers, Charlene / Adriaana Jacobs / Adrian L.V. Davis / Andrew B. Davies / Ansie S. Dippenaar-Schoeman / Antoinette P. Malan / Antoinette Swart / Ariella N. Rink / Brigitte Braschler / Candice Jansen van Rensburg / Charles Griffiths / Charles R. Haddad / Danuta J. Plisko / David G. Herbert / Driekie Fourie / Eddie Ueckermann / Elizabeth A. Hugo-Coetzee / Grant A. Duffy / Jan-Andries Neethling /

Pedobiologia. 2016 May, v. 59, no. 3

2016

Abstract: Soils are integral to agricultural productivity, biodiversity, and the maintenance of ecosystem services. However, soil ecosystem research depends on foundational biological knowledge that is often missing. In this review, we present a comprehensive, ... ...

Abstract	Soils are integral to agricultural productivity, biodiversity, and the maintenance of ecosystem services. However, soil ecosystem research depends on foundational biological knowledge that is often missing. In this review, we present a comprehensive, cross-taxa overview of the soil biota of South Africa. We discuss the literature and sampling methods used to assess soil biota, the available taxonomic expertise and main collections within South Africa, the availability of identification guides and online resources, and the status and distribution of described species. We include species lists for all South African soil biota and, for groups with sufficient distribution records, species richness maps. Despite South Africa being only 0.8% of the earth’s terrestrial area, it contains nearly 1.8% of the world’s described soil species (mean per taxon 3.64%, range 0.17–15%; n=36 groups), with nematodes and earthworms showing a remarkable (6.4 and 7.7%) proportion of globally described diversity. Endemism is high for most groups, ranging from 33–92%. However, major knowledge gaps exist for most soil biota groups. While sampling has been relatively comprehensive in some areas for a few groups (particularly those with direct socioeconomic impacts), the Nama-Karoo, Northern Cape and Eastern Cape are poorly sampled. Natural soils in biodiversity hotspots, such as the Fynbos Biome, are also understudied. We argue that a more integrative approach to acquiring foundational knowledge in soil biodiversity is needed if applied soil research is to be effective in ensuring sustainable soil health. Considerable investment will be required to bring our understanding of the soil biodiversity in this megadiverse region to a level where the Millennium Development Goals can be reached.
Keywords	earthworms ; ecosystem services ; fynbos ; indigenous species ; Nematoda ; soil ; soil ecosystems ; soil quality ; species diversity ; South Africa
Language	English
Dates of publication	2016-05
Size	p. 129-174.
Publishing place	Elsevier GmbH
Document type	Article
ZDB-ID	207680-9
ISSN	1873-1511 ; 0031-4056
ISSN (online)	1873-1511
ISSN	0031-4056
DOI	10.1016/j.pedobi.2016.03.004
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Chronic Activation of γ2 AMPK Induces Obesity and Reduces β Cell Function.

Yavari, Arash / Stocker, Claire J / Ghaffari, Sahar / Wargent, Edward T / Steeples, Violetta / Czibik, Gabor / Pinter, Katalin / Bellahcene, Mohamed / Woods, Angela / Martínez de Morentin, Pablo B / Cansell, Céline / Lam, Brian Y H / Chuster, André / Petkevicius, Kasparas / Nguyen-Tu, Marie-Sophie / Martinez-Sanchez, Aida / Pullen, Timothy J / Oliver, Peter L / Stockenhuber, Alexander /

Nguyen, Chinh / Lazdam, Merzaka / O'Dowd, Jacqueline F / Harikumar, Parvathy / Tóth, Mónika / Beall, Craig / Kyriakou, Theodosios / Parnis, Julia / Sarma, Dhruv / Katritsis, George / Wortmann, Diana D J / Harper, Andrew R / Brown, Laurence A / Willows, Robin / Gandra, Silvia / Poncio, Victor / de Oliveira Figueiredo, Márcio J / Qi, Nathan R / Peirson, Stuart N / McCrimmon, Rory J / Gereben, Balázs / Tretter, László / Fekete, Csaba / Redwood, Charles / Yeo, Giles S H / Heisler, Lora K / Rutter, Guy A / Smith, Mark A / Withers, Dominic J / Carling, David / Sternick, Eduardo B / Arch, Jonathan R S / Cawthorne, Michael A / Watkins, Hugh / Ashrafian, Houman

Cell metabolism

2016 Volume 23, Issue 5, Page(s) 821–836

Abstract: Despite significant advances in our understanding of the biology determining systemic energy homeostasis, the treatment of obesity remains a medical challenge. Activation of AMP-activated protein kinase (AMPK) has been proposed as an attractive strategy ... ...

Abstract	Despite significant advances in our understanding of the biology determining systemic energy homeostasis, the treatment of obesity remains a medical challenge. Activation of AMP-activated protein kinase (AMPK) has been proposed as an attractive strategy for the treatment of obesity and its complications. AMPK is a conserved, ubiquitously expressed, heterotrimeric serine/threonine kinase whose short-term activation has multiple beneficial metabolic effects. Whether these translate into long-term benefits for obesity and its complications is unknown. Here, we observe that mice with chronic AMPK activation, resulting from mutation of the AMPK γ2 subunit, exhibit ghrelin signaling-dependent hyperphagia, obesity, and impaired pancreatic islet insulin secretion. Humans bearing the homologous mutation manifest a congruent phenotype. Our studies highlight that long-term AMPK activation throughout all tissues can have adverse metabolic consequences, with implications for pharmacological strategies seeking to chronically activate AMPK systemically to treat metabolic disease.
MeSH term(s)	AMP-Activated Protein Kinases/metabolism ; Adiposity/genetics ; Adult ; Aging/pathology ; Agouti-Related Protein/metabolism ; Animals ; Arcuate Nucleus of Hypothalamus/metabolism ; Energy Metabolism/genetics ; Enzyme Activation ; Feeding Behavior ; Female ; Heterozygote ; Humans ; Hyperphagia/complications ; Hyperphagia/enzymology ; Hyperphagia/genetics ; Hyperphagia/pathology ; Hypothalamus/metabolism ; Insulin/metabolism ; Insulin-Secreting Cells/enzymology ; Insulin-Secreting Cells/pathology ; Male ; Mice ; Mitochondria/metabolism ; Mutation/genetics ; Neurons/metabolism ; Obesity/blood ; Obesity/complications ; Obesity/enzymology ; Obesity/pathology ; Oxidative Phosphorylation ; Receptors, Ghrelin/metabolism ; Ribosomes/metabolism ; Signal Transduction/genetics ; Transcriptome/genetics ; Up-Regulation/genetics
Chemical Substances	Agouti-Related Protein ; Insulin ; Receptors, Ghrelin ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2016-04-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2176834-1
ISSN	1932-7420 ; 1550-4131
ISSN (online)	1932-7420
ISSN	1550-4131
DOI	10.1016/j.cmet.2016.04.003
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Review article. Soil biota in a megadiverse country: Current knowledge and future research directions in South Africa

Janion-Scheepers, Charlene / Measey, John / Braschler, Brigitte / Chown, Steven L. / Coetzee, Louise / Colville, Jonathan F. / Dames, Joanna / Davies, Andrew B. / Davies, Sarah J. / Davis, Adrian / Dippenaar-Schoeman, Ansie S. / Duffy, Grant A. / Fourie, Driekie / Griffiths, Charles / Haddad, Charles R. / Hamer, Michelle / Herbert, David G. / Hugo-Coetzee, Elizabeth A. / Jacobs, Adriaana /

Pedobiologia

2016 Volume 59, Issue 3, Page(s) 129

Language	German ; English
Document type	Article
ZDB-ID	207680-9
ISSN	0031-4056
DOI	10.1016/j.pedobi.2016.03.004
Database	Current Contents Nutrition, Environment, Agriculture

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