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. 2023 Feb 15;14:1114582. doi: 10.3389/fimmu.2023.1114582

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Copyright © 2023 Keerthana, Rayginia, Shifana, Anto, Kalimuthu, Isakov and Anto

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Graphical representation of the domain structure and isoforms of AMPK. The three sub-units, namely, αβγ, which constitute the heterotrimeric complex structure of AMPK have different isoforms. While the α and β sub-units have two isoforms each, the γ sub-unit has three isoforms. Thr, threonine; Ser, Serine; AID, Autoinhibitory domain; ST-loop, Stem loop; CTD, C-terminal domain; αRIM1/2, α-subunit motifs; α/β linker, regulatory linker region; GBD, GTPase protein binding domain; CBS1 domain, Cystathionine beta synthase1 domain; CBS2 domain, Cystathionine beta synthase2 domain; CBS3 domain, Cystathionine beta synthase3 domain; CBS4 domain, Cystathionine beta synthase 4 domain AMP, Adenosine monophosphate; ADP, Adenosine diphosphate; ATP, Adenosine triphosphate.