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. 2020 Dec 4;11(12):1033. doi: 10.1038/s41419-020-03246-7

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© The Author(s) 2020

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Fig. 3 — Under unstressed conditions, AMPKα remains ubiquitylated; ubiquitination of AMPK inhibits its phosphorylation and activation. Upon cellular stress, AMP/ADP binding to AMPKg leads to partial activation of AMPK and phosphorylation of USP10. Deubiquitination of AMPK by USP10 contributes to AMPK phosphorylation and activation by LKB1. Parallelly, activated AMPK phosphorylates USP10 thus enhancing its activity under stress thus amplifying AMPK activation.