RanBPM is an L1-interacting protein that regulates L1-mediated mitogen-activated protein kinase activation
| Autor: | Ling, Cheng, Sandra, Lemmon, Vance, Lemmon |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Nuclear Proteins
Article Protein Structure Tertiary Enzyme Activation Cytoskeletal Proteins ran GTP-Binding Protein Two-Hybrid System Techniques COS Cells Chlorocebus aethiops Neurites Animals Drug Interactions Tissue Distribution Mitogen-Activated Protein Kinases Leukocyte L1 Antigen Complex Adaptor Proteins Signal Transducing |
| Zdroj: | Journal of neurochemistry. 94(4) |
| ISSN: | 0022-3042 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text