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Updated: Aug 9, 2026

Metabolic Labeling of Leucine Rich Repeat Kinases 1 and 2 with Radioactive Phosphate
Published on: September 18, 2013
MAP kinase pathway-dependent phosphorylation of the L1-CAM ankyrin binding site regulates neuronal growth
John D Whittard1, Takeshi Sakurai, Melanie R Cassella
1Department of Pharmacology and Biological Chemistry, Mt. Sinai School of Medicine, New York, NY 10029, USA.
Abstract:
The growth of neuronal processes depends critically on the function of adhesion proteins that link extracellular ligands to the cytoskeleton. The neuronal adhesion protein L1-CAM serves as a receptor for nerve growth-promoting proteins, a process that is inhibited by the interaction between L1-CAM and the cytoskeleton adaptor ankyrin. Using a novel reporter based on intramolecular bioluminescence resonance energy transfer, we have determined that the MAP kinase pathway regulates the phosphorylation of the FIGQY motif in the adhesion protein L1-CAM and its interaction with ankyrin B. MAP kinase pathway inhibitors block L1-CAM-mediated neuronal growth. However, this blockade is partially rescued by inhibitors of L1-CAM-ankyrin binding. These results demonstrate that the MAP kinase pathway regulates L1-CAM-mediated nerve growth by modulating ankyrin binding, suggesting that nerve growth can be regulated at the level of individual receptors.
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