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MBC in Press, published online ahead of print April 5, 2006
Mol. Biol. Cell 10.1091/mbc.E06-01-0090

A more recent version of this article appeared on June 1, 2006
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Submitted on January 31, 2006
Revised on March 23, 2006
Accepted on March 27, 2006

MAP Kinase Pathway-dependent Phosphorylation of the L1-CAM Ankyrin-binding Site Regulates Neuronal Growth

John D. Whittard, Takeshi Sakurai, Melanie R. Cassella, Mihaela Gazdoiu, and Dan P. Felsenfeld

Department of Pharmacology and Biological Chemistry, Mt. Sinai School of Medicine, New York, NY 10029

Monitoring Editor: Paul Forscher

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 (Gil et al., 2003). Using a novel reporter based on intramolecular bioluminescence resonance energy transfer (BRET), 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.

Address correspondence to: Dan P. Felsenfeld (dan.felsenfeld{at}mssm.edu)




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