NTF4-bound NTRK2 dimers trans-autophosphorylate

NTF4-induced dimerization of the receptor tyrosine kinase NTRK2 (TRKB), similar to BDNF-induced dimerization, leads to trans-autophosphorylation of NTRK2. NTF4-induced phosphorylation of NTRK2 on tyrosine residue Y516 was demonstrated using mouse Ntrk2 (human Y516 corresponds to Y515 of mouse Ntrk2). As the electrophoretic migration pattern of Ntrk2 phosphorylated in response to NTF4 is indistinguishable from the electrophoretic migration pattern of Ntrk2 phosphorylated in response to BDNF, and identical downstream effectors are activated, it is assumed that NTF4 induces phosphorylation of NTRK2 on five evolutionarily conserved tyrosine residues in the cytoplasmic tail of NTRK2: Y516, Y702, Y706, Y707 and Y817 (Minichiello et al. 1998).

NTF4诱导的受体酪氨酸激酶NTRK2（TRKB）的二聚化，与BDNF诱导的二聚化相似，导致NTRK2的跨自磷酸化。通过小鼠Ntrk2（人Y516对应于小鼠Ntrk2的Y515）证实了NTF4诱导NTRK2在酪氨酸残基Y516上的磷酸化。由于NTF4诱导的Ntrk2磷酸化在电泳迁移模式上与BDNF诱导的Ntrk2磷酸化在电泳迁移模式上无区别，并且激活了相同的下游效应器，因此推断NTF4可诱导NTRK2在细胞质尾部的五个进化保守的酪氨酸残基（Y516、Y702、Y706、Y707和Y817）上的磷酸化（Minichiello等，1998年）。