Extended Data Fig. 6: mTORC1 phosphorylates AMPKα2 S377.

a, Repeated measures correlation profile of AMPK S377 (two-sided, BH-adjusted p-value). b, Quantification of phosphosites on AMPK from in vitro kinase assays with mTORC1 and different combinations of AMPK subunits. The γ subunit was kept as AMPKγ1. For each condition, n = 1. c, AMPK inhibitory site profiles in human skeletal muscle. d, Sequence alignment of AMPKα2 S377 across different species. S. cerevisiae SNF1 was used in the alignment. e, AMPKα2β2γ1 structure from PDB 6b2e. AMPKα2 residues 377–398 were not modelled so are included as a dashed line. AMPKα2 S377 is approximated as immediately adjacent to residue 376 and indicated in green. f, Real-time proliferation analysis of AMPKα1/2 KO MEF cells re-expressing WT or S377A AMPKα2 in media with 25 mM glucose. g, AMPK substrate phosphosite profiles in human skeletal muscle. h, mTORC1 substrate phosphosite profiles in human skeletal muscle. Data are presented as the mean +/− SEM represented by shading.