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Ethanol interacts with an alcohol binding pocket in the L1 extracellular domain (ECD), and dephosphorylation of S1248 in the L1 cytoplasmic domain (CD) renders L1 adhesion insensitive to inhibition by ethanol (L1 insensitive). The mechanism underlying this inside\u2010out signaling is unknown. Here we show that phosphorylation of the human L1\u2010CD at S1152, Y1176, S1181, and S1248 renders L1 sensitive to ethanol by promoting L1 coupling with ankyrin\u2010G and the spectrin\u2010actin cytoskeleton. Knockdown of ankyrin\u2010G or L1 mutations that uncouple L1 from ankyrin reduce L1 sensitivity to ethanol, but not methanol, consistent with a small conformational change in the extracellular alcohol binding pocket. Phosphorylation of Y1176 and ankyrin\u2010G coupling with L1 are higher in NIH\/3T3 clonal cell lines in which ethanol inhibits L1 adhesion than in ethanol\u2010resistant NIH\/3T3 clonal cell lines. Similarly, phosphorylation of Y1176 is higher in C57BL\/6J mice that are sensitive to ethanol teratogenesis than in ethanol resistant C57BL\/6N mice. Finally, polymorphisms in genes that encode ankyrin\u2010G and p90rsk, a kinase that phosphorylates S1152, are linked to facial dysmorphology in children with heavy prenatal ethanol exposure. These findings indicate that genes that regulate L1 coupling to ankyrin may influence susceptibility to FASD.\u2014Dou, X., Menkari, C., Mitsuyama, R., Foroud, T., Wetherill, L., Hammond, P., Suttie, M., Chen, X., Chen, S.\u2010Y., Charness, M. E., Collaborative Initiative on Fetal Alcohol Spectrum Disorders. L1 coupling to ankyrin and the spectrin\u2010actin cytoskeleton modulates ethanol inhibition of L1 adhesion and ethanol teratogenesis. 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