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.Snf1/腺苷酸活化蛋白激酶（AMP-activated protein kinase, AMPK）以异源三聚体复合物形式行使功能，其组成包括感知细胞能量状态的调节亚基、带有经典激酶结构域的催化亚基，以及用于稳定复合物的支架亚基。鉴于酵母Snf1与哺乳动物AMPK在序列、结构与功能上均存在高度保守性，探究这两类激酶所调控的下游效应的保守程度便具有了充分的研究合理性。