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Redox implications of AMPK-mediated signal transduction beyond energetic clues

Open access
Cardaci, Simone, Filomeni, Giuseppe, Ciriolo, Maria Rosa·2012·Journal of Cell Science

Abstract

Since the discovery of AMP-dependent protein kinase (AMPK), its fundamental role in regulating metabolic pathways and the molecular mechanism underlying the regulation of its activity by adenine nucleotides has been widely studied. AMPK is not only an energy-responsive enzyme, but it also senses redox signals. This review aims at recapitulating the recent lines of evidence that demonstrate the responsiveness of this kinase to metabolic and nitroxidative imbalance, thus providing new insights into the intimate networks of redox-based signals upstream of AMPK. In particular, we discuss its well-recognized activation downstream of mitochondrial dysfunction, debate the recent findings that AMPK is directly targeted by pro-oxidant species, and question alternative redox pathways that allow AMPK to be included into the large class of redox-sensing proteins. The possible therapeutic implications of the role of AMPK in redox-associated pathologies, such as cancer and neurodegeneration, are also discussed in light of recent advances that suggest a role for AMPK in the tuning of redox-dependent processes, such as apoptosis and autophagy.

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Metadata

Authors
Cardaci, S., Filomeni, G., & Ciriolo, M. R.
Venue
Journal of Cell Science
Published
2012-01-01
Volume
125
Issue
Pt 9
Pages
2115-25
ISSN
  • 0021-9533 (ISSN-L)
  • 1477-9137
OpenAlex
W2008004470
Cited by
197
References
29
FWCI
6.39
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Redox implications of AMPK-mediated signal transduction beyond energetic clues. https://app.cochat.ai/papers/10.1242/jcs.095216
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Cardaci, S., Filomeni, G., & Ciriolo, M. R. (2012). Redox implications of AMPK-mediated signal transduction beyond energetic clues. Journal of Cell Science. https://doi.org/10.1242/jcs.095216

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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