RanBPM is an L1-interacting protein that regulates L1-mediated mitogen-activated protein kinase activation.
A yeast two-hybrid screen using the last 28 amino acids of the cytoplasmic domain of the neural cell adhesion molecule L1 identified RanBPM as an L1-interacting protein. RanBPM associates with L1 in vivo and the N-terminal region of RanBPM (N-RanBPM), containing the SPRY domain, is sufficient for the interaction with ... L1 in a glutathione S-transferase pull-down assay. L1 antibody patching dramatically changes the subcellular localization of N-RanBPM in transfected COS cells. Overexpression of N-RanBPM in COS cells reduces L1-triggered extracellular signal-regulated kinase 1/2 activation by 50% and overexpression of N-RanBPM in primary neurons inhibits L1-mediated neurite outgrowth and branching. These data suggest that RanBPM is an adaptor protein that links L1 to the extracellular signal-regulated kinase/MAPK pathway.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Animals, COS Cells, Cercopithecus aethiops, Cytoskeletal Proteins, Drug Interactions, Enzyme Activation, Leukocyte L1 Antigen Complex, Mitogen-Activated Protein Kinases, Neurites, Nuclear Proteins, Protein Structure, Tertiary, Tissue Distribution, Two-Hybrid System Techniques, ran GTP-Binding Protein
Adaptor Proteins, Signal Transducing, Animals, COS Cells, Cercopithecus aethiops, Cytoskeletal Proteins, Drug Interactions, Enzyme Activation, Leukocyte L1 Antigen Complex, Mitogen-Activated Protein Kinases, Neurites, Nuclear Proteins, Protein Structure, Tertiary, Tissue Distribution, Two-Hybrid System Techniques, ran GTP-Binding Protein
J. Neurochem.
Date: Aug. 01, 2005
PubMed ID: 16000162
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