Data from: The inhibitory SAPS3 – AMPK interaction detected in HEK293 cells is not detectable in muscle or liver from humans or mice

It has been proposed that the regulatory Sit4-associated protein subunit 3
(SAPS3) of protein phosphatase 6 (PP6C) acts as an AMP-activated protein
kinase (AMPK) inhibitor by recruiting PP6C to dephosphorylate AMPKα-T172.
While we confirm this interaction in HEK293 cells, we find limited
evidence for a SAPS3–AMPK interaction in metabolically perturbed liver and
skeletal muscle from humans and mice. Across fasting, high-fat diet
feeding, and exercise conditions, co-immunoprecipitation assays failed to
detect endogenous SAPS3–AMPK and PP6C–AMPK interactions. These findings
challenge the physiological relevance of SAPS3/PP6C as regulators of AMPK
in mature tissues and highlight the need for further investigation into
the regulation of AMPK by protein phosphatases in vivo.