Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 19, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/ijms19113534
Keywords
energy metabolism; AMPK; activation loop; AID; -linker; -linker; CBS; LKB1; CaMKK2; RIM
Funding
- Van Andel Research Institute
- National Institutes of Health [R01 GM129436]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM129436] Funding Source: NIH RePORTER
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Adenosine monophosphate (AMP)-activated protein kinase (AMPK) is a heterotrimeric complex that functions as a central regulator of energy homeostasis. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs. AMPK senses the cellular energy state by competitive binding of the three adenine nucleotides AMP, ADP, and ATP to three sites in its subunit, each, which in turn modulates the activity of AMPK's kinase domain in its subunit. Our current understanding of adenine nucleotide binding and the mechanisms by which differential adenine nucleotide occupancies activate or inhibit AMPK activity has been largely informed by crystal structures of AMPK in different activity states. Here we provide an overview of AMPK structures, and how these structures, in combination with biochemical, biophysical, and mutational analyses provide insights into the mechanisms of adenine nucleotide binding and AMPK activity modulation.
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