Many small molecules induce general anesthesia in animals ranging from insects to mammals. Although their mechanism of action remains controversial, it is known that a compound's efficacy as an anesthetic is strongly predicted by both its hydrophobicity and its potency in inhibiting a wide variety of ligand gated ion channels. Here I will argue that anesthetics interfere with and mimic native regulation of ion channels by their two-dimensional solvent, the plasma membrane, which is tuned close to a liquid-liquid critical point. I will first review the evidence suggesting that plasma membranes are indeed tuned close to such a de-mixing critical point. I will then report on recent experiments where we show that the n-alcohol anesthetics take plasma membrane derived vesicles away from criticality by lowering their critical temperature, with 'intoxication reversers' acting opposite, raising Tc. I will then discuss our model for understanding anesthetic effects, in which the nearly critical membrane's order parameter acts as an allosteric modulator for bound channels. I will show simulation results from the 2D-Ising model that suggest that ion channels could indeed be strongly affected by our measured changes in critical temperatures. Our model predicts that anesthetic sensitive channels will have their membrane environment modified by activation, a prediction we are building up to test.