Article
A novel mutation within the extracellular domain of TrkA causes constitutive receptor activation.
Oncogene - 8 Mar 2001
Arevalo J C, Conde B, Hempstead B I, Chao M V, Martín-Zanca D, Pérez P
Abstract excerpt
The TrkA NGF receptor extracellular region contains three leucine repeats flanked by cysteine clusters and two immunoglobulin-like domains that are required for specific ligand binding. Deletion of the immunoglobulin-like domains abolishes NGF binding and causes ligand independent activation of the receptor. Here we report a specific mutation that increases the binding affinity of the TrkA receptor for NGF. A...
Topics
- Amino Acid Substitution
- Animals
- Binding Sites
- Colony-Forming Units Assay
- Ligands
- Mutagenesis, Site-Directed
- Mutation
- Nerve Growth Factor
- Neurites
- PC12 Cells
- Phosphorylation