Deletion of cytoplasmic sequences of the nerve growth factor receptor leads to loss of high affinity ligand binding

摘要: Abstract The nerve growth factor (NGF) receptor is a glycosylated transmembrane protein present on the cell surface as both high and low affinity forms, but biological responsiveness requires interactions of NGF with site. We have tested effects mutations in intracellular domain upon its expression equilibrium binding 125I-NGF. Although mutant receptors lacking entire cytoplasmic are processed expressed at capable to NGF, absence sequences leads loss lack an appropriate cross-linking pattern assessed by N-hydroxysuccinimidyl 4-azidobenzoate photoaffinity cross-linking. These results, taken together highly conserved nature these sequences, implies that interaction accessory molecule necessary form receptor.