Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 17, Issue 6, Pages 2696-2706Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.e06-01-0090
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Funding
- NIGMS NIH HHS [R01 GM063192, R0-1 GM63192] Funding Source: Medline
- NINDS NIH HHS [R01 NS041687, R0-1 NS41687] Funding Source: Medline
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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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