Abstract
SummaryThe maintenance of energetic homeostasis in the face of limited available nutrients is a complex problem faced by all organisms. One important mechanism to maintain energetic homeostasis involves the activation of the energy sensor AMP-activated protein kinase (AMPK). AMPK is a cell-autonomous energy sensor that is highly sensitive to and regulated by the ATP to ADP and ATP to AMP ratios. However, the genetic analysis of AMPK signaling in vertebrates has been complicated by the existence of multiple redundant AMPK subunits. Here, we describe the identification of mutations in the single Drosophila melanogaster AMPK catalytic subunit (AMPKα) and their implications for neural maintenance and integrity. This article provides a citation replacement for previously published ampkα alleles, transgenes and neuronal phenotypes, which remain accurate; however, they were used in a previously published study that has subsequently been retracted (Mirouse et al., 2013).
Highlights
AMP-activated protein kinase (AMPK) acts as a cellular energy sensor and is activated by ADP and AMP, which accumulate when ATP levels are low (Braco et al, 2012; Johnson et al, 2010; Kahn et al, 2005)
Summary The maintenance of energetic homeostasis in the face of limited available nutrients is a complex problem faced by all organisms
One important mechanism to maintain energetic homeostasis involves the activation of the energy sensor AMP-activated protein kinase (AMPK)
Summary
AMP-activated protein kinase (AMPK) acts as a cellular energy sensor and is activated by ADP and AMP, which accumulate when ATP levels are low (Braco et al, 2012; Johnson et al, 2010; Kahn et al, 2005). AMPK is implicated in a number of signaling pathways (Hardie, 2004; Hardie, 2007; Shaw, 2009). AMPK signaling acts downstream to inhibit protein and lipid synthesis, for example, activating elongation factor-2 kinase, which causes inhibition of the elongation step of translation (Horman et al, 2002; Winder et al, 1997); inhibiting the target-of-rapamycin (TOR) pathway, which stimulates the initiation step of protein synthesis by the phosphorylation of multiple targets (Proud, 2004); and phosphorylating and inhibiting the fatty acid synthesis and rate-limiting enzyme
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