Mammalian AMP-activated protein kinase has only a partial functional redundancy with Snf1 in Saccharomyces cerevisiae

Snf1/AMPK functions as a heterotrimeric complex, consisting of a regulatory subunit that is senses the energy status, a catalytic subunit with the canonical kinase domain and a scaffolding subunit to secure the complex together. The high degree of conservation in the sequence, structure and function of yeast Snf1 and mammalian AMPK, it is only logical to investigate the extent of conservation in the downstream effects that are controlled by these kinases. The reference yeast strain is the mutant strain snf1Δ carrying the plasmid HA-Snf1. The mutant strain Alpha1 is the mutant strain snf1Δ carrying the plasmid HA-Alpha1, which is the katalytic domain of Alpha1 subunit of AMPK fused to the regulatory domain of Snf1. The mutant strain HA-T210A is the mutant strain snf1Δ carrying the plasmid HA-T210A, which is the native Snf1 but Thr210 (the phosphorylation and activation site) was mutated into Ala.