Department of Nutrition, Dietetics, and Hospitality Management, Auburn University, Auburn, AL 36849, USA.
Biochem Biophys Res Commun. 2012 May 4;421(2):286-90. doi: 10.1016/j.bbrc.2012.04.001. Epub 2012 Apr 7.
Specific binding of nerve growth factor (NGF) to p75 neurotrophin receptor (p75(NTR)) leads to p75(NTR) polyubiquitination and its subsequent interaction with TRAF6 resulting in neuronal cell survival. However, when the binding of NGF to p75(NTR) was blocked with p75 antiserum, p75(NTR) polyubiquitination and neuronal cell survival were impaired. Results showed that tyrosine phosphorylation of p75(NTR) increased the polyubiquitination of p75(NTR) and contributed to the observed apparent neuroprotective effects. Similar to p75(NTR) polyubiquitination, interaction of TRAF6 with p75(NTR) was NGF/tyrosine phosphorylation dependent suggesting that TRAF6 might function as an E3 ubiquitin ligase. In sum, the results show that specific binding of NGF to p75(NTR) mediates neuronal cell survival.
神经生长因子（NGF）与 p75 神经生长因子受体（p75(NTR))) 的特异性结合导致 p75(NTR)多泛素化，随后与 TRAF6 相互作用，导致神经元细胞存活。然而，当用 p75 抗血清阻断 NGF 与 p75(NTR) 的结合时，p75(NTR)多泛素化和神经元细胞存活受损。结果表明，p75(NTR)的酪氨酸磷酸化增加了 p75(NTR)的多泛素化，并有助于观察到的明显的神经保护作用。与 p75(NTR)多泛素化类似，TRAF6 与 p75(NTR)的相互作用依赖于 NGF/酪氨酸磷酸化，表明 TRAF6 可能作为 E3 泛素连接酶发挥作用。总之，这些结果表明，NGF 与 p75(NTR)的特异性结合介导神经元细胞存活。
