AMP-activated protein kinase - the key sensor of cellular energy charge

2001 ◽  
Vol 33 (6) ◽  
pp. A146 ◽  
Author(s):  
D.Grahame Hardie
Keyword(s):  
Protein Kinase ◽  
Energy Charge ◽  
Cellular Energy ◽  
Amp Activated Protein Kinase

scholarly journals AMP-activated protein kinase: an ultrasensitive system for monitoring cellular energy charge

1999 ◽  
Vol 338 (3) ◽  
pp. 717 ◽  
Author(s):  
D. Grahame HARDIE ◽  
Ian P. SALT ◽  
Simon A. HAWLEY ◽  
Stephen P. DAVIES
Keyword(s):  
Protein Kinase ◽  
Energy Charge ◽  
Cellular Energy ◽  
Amp Activated Protein Kinase

scholarly journals AMP-activated protein kinase: an ultrasensitive system for monitoring cellular energy charge

1999 ◽  
Vol 338 (3) ◽  
pp. 717-722 ◽  
Author(s):  
D. Grahame HARDIE ◽  
Ian P. SALT ◽  
Simon A. HAWLEY ◽  
Stephen P. DAVIES
Keyword(s):  
Protein Kinase ◽  
Energy Charge ◽  
Fold Increase ◽  
Maximal Activity ◽  
Hill Coefficient ◽  
Intact Cells ◽  
Cellular Energy ◽  
Critical Range ◽  
Kinase Cascade ◽  
Amp Activated Protein Kinase

The AMP-activated protein kinase cascade is activated by elevation of AMP and depression of ATP when cellular energy charge is compromised, leading to inhibition of anabolic pathways and activation of catabolic pathways. Here we show that the system responds in intact cells in an ultrasensitive manner over a critical range of nucleotide concentrations, in that only a 6-fold increase in activating nucleotide is required in order for the maximal activity of the kinase to progress from 10% to 90%, equivalent to a co-operative system with a Hill coefficient (h) of 2.5. Modelling suggests that this sensitivity arises from two features of the system: (i) AMP acts at multiple steps in the cascade (multistep sensitivity); and (ii) the upstream kinase is initially saturated with the downstream kinase (zero-order ultrasensitivity).

AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins

2003 ◽  
Vol 31 (1) ◽  
pp. 224-227 ◽  
Author(s):  
T. Leff
Keyword(s):  
Gene Expression ◽  
Transcription Factors ◽  
Protein Kinase ◽  
Gene Transcription ◽  
Metabolic Pathways ◽  
Energy Charge ◽  
Nuclear Proteins ◽  
Cellular Energy ◽  
Ampk Activity ◽  
Amp Activated Protein Kinase

One of the primary functions of AMP-activated protein kinase (AMPK) is to regulate the metabolic pathways in response to reduced cellular energy charge. Most of the known targets of the kinase are cytoplasmic enzymes involved in both catabolic and anabolic metabolism. In addition, activation of AMPK in many cells results in changes in the pattern of gene expression. Although some of these effects are undoubtedly secondary responses to modified cellular metabolism, it is possible that in addition to its well-characterized function in the cytoplasm, AMPK also directly phosphorylates and regulates proteins involved in gene transcription. There are now several examples of transcription factors, cofactors and components of the transcriptional core machinery that are directly phosphorylated and regulated by AMPK. Here I review these examples and discuss the significance of AMPK activity in the nucleus.

scholarly journals Regulation of the energy sensor AMP-activated protein kinase by antigen receptor and Ca2+ in T lymphocytes

2006 ◽  
Vol 203 (7) ◽  
pp. 1665-1670 ◽  
Author(s):  
Peter Tamás ◽  
Simon A. Hawley ◽  
Rosemary G. Clarke ◽  
Kirsty J. Mustard ◽  
Kevin Green ◽  
...  
Keyword(s):  
Protein Kinase ◽  
T Lymphocytes ◽  
Energy Homeostasis ◽  
Antigen Receptor ◽  
Adenosine Monophosphate ◽  
Ampk Activation ◽  
Serine Kinase ◽  
Cellular Energy ◽  
Amp Activated Protein Kinase ◽  
Stimulation Of

The adenosine monophosphate (AMP)–activated protein kinase (AMPK) has a crucial role in maintaining cellular energy homeostasis. This study shows that human and mouse T lymphocytes express AMPKα1 and that this is rapidly activated in response to triggering of the T cell antigen receptor (TCR). TCR stimulation of AMPK was dependent on the adaptors LAT and SLP76 and could be mimicked by the elevation of intracellular Ca2+ with Ca2+ ionophores or thapsigargin. AMPK activation was also induced by energy stress and depletion of cellular adenosine triphosphate (ATP). However, TCR and Ca2+ stimulation of AMPK required the activity of Ca2+–calmodulin-dependent protein kinase kinases (CaMKKs), whereas AMPK activation induced by increased AMP/ATP ratios did not. These experiments reveal two distinct pathways for the regulation of AMPK in T lymphocytes. The role of AMPK is to promote ATP conservation and production. The rapid activation of AMPK in response to Ca2+ signaling in T lymphocytes thus reveals that TCR triggering is linked to an evolutionally conserved serine kinase that regulates energy metabolism. Moreover, AMPK does not just react to cellular energy depletion but also anticipates it.

scholarly journals AMP-activated protein kinase adapts rRNA synthesis to cellular energy supply

2009 ◽  
Vol 106 (42) ◽  
pp. 17781-17786 ◽  
Author(s):  
S. Hoppe ◽  
H. Bierhoff ◽  
I. Cado ◽  
A. Weber ◽  
M. Tiebe ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Energy Supply ◽  
Rrna Synthesis ◽  
Cellular Energy ◽  
Amp Activated Protein Kinase

scholarly journals AMP-activated protein kinase connects cellular energy metabolism to KATP channel function

2012 ◽  
Vol 52 (2) ◽  
pp. 410-418 ◽  
Author(s):  
Hidetada Yoshida ◽  
Li Bao ◽  
Eirini Kefaloyianni ◽  
Eylem Taskin ◽  
Uzoma Okorie ◽  
...  
Keyword(s):  
Energy Metabolism ◽  
Protein Kinase ◽  
Katp Channel ◽  
Cellular Energy ◽  
Cellular Energy Metabolism ◽  
Channel Function ◽  
Amp Activated Protein Kinase
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