NGFR (Nerve Growth Factor Receptor, TNFR super family, member 16, LNGFR, p75 neurotrophin receptor) is important for the development, differentiation, and survival of variety of neuronal and non-neuronal cells. NGF action is mediated by binding two distinct receptors, the high affinity p140 and low affinity Nerve Growth Factor (NGF) Receptor (p75NGFR) or Neurotrophin Receptor (p75NTR). NGFR contains an extracellular domain containing four 40-amino acid repeats with 6 cysteine residues at conserved positions followed by a serine/threonine-rich region, a single transmembrane domain, and a 155-amino acid cytoplasmic domain. The cysteine-rich region contains the nerve growth factor binding domain. Neurotrophic factors control the survival, differentiation and maintenance of neurons in the peripheral and central nervous systems, and of other neural crest-derived cell types. Developing sympathetic neurons are absolutely dependent upon nerve growth factor during the period of target competition in vivo. Antibodies reacting specifically with NGFR p75 are useful tools in the detection and characterization of NGFR p75, to enhance our understanding of a wide range of phenomena in the development, plasticity and repair of the nervous system.
NGFR can also associate with other NGF receptors such as Trk through the cytosolic and transmembrane domains and thus can function as a co-receptor that refines Trk affinity and specificity for neurotrophins. Finally, upon binding of various neurotrophins, NGFR associates with tumor necrosis factor receptor-6 (TRAF6), suggesting that it can potentially function as a signal transducer for NGF signals through NGFR. NGFR may play a role in the development of cancer stem cells in melanoma and other cancer types.