Phosphorylation at Tyr-694 of Nogo-A by Src-family kinases.
Phosphorylation at Tyr-694 of Nogo-A by Src-family kinases.
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DOI：
10.1016/j.bbrc.2006.09.007
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发表时间：
2006-11
影响因子：
3.1
通讯作者：
Kazumasa Yokoyama;T. Tezuka;N. Hoshina;T. Nakazawa;Tadashi Yamamoto
中科院分区：
文献类型：
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作者：
Kazumasa Yokoyama;T. Tezuka;N. Hoshina;T. Nakazawa;Tadashi Yamamoto
Nogo-A是中枢神经系统中与髓磷脂相关的神经突生长抑制蛋白。出乎意料的是，在小鼠中靶向破坏Nogo-A导致很少或没有轴突再生的改善，这表明Nogo-A有其他功能和/或接受复杂的调控来发挥其抑制功能。在这里，我们发现Nogo-A在n端区域的tyr694发生磷酸化。磷酸化是由src家族酪氨酸激酶共同介导的，这些酪氨酸激酶在神经系统中起着许多重要作用。Nogo-A的酪氨酸磷酸化水平似乎与少突胶质细胞的发育阶段无关，可能受到特定的细胞外刺激的调节。鉴定Nogo-A的酪氨酸磷酸化将为Nogo-A的功能引入额外的复杂性。
Nogo-A is a neurite outgrowth inhibitor protein associated with myelin in the central nervous system. Unexpectedly, targeted disruption of Nogo-A in mice results in little or no improvement of axonal regeneration, suggesting that Nogo-A has other functions and/or receives complex regulations to exert its inhibitory functions. Here, we have found that Nogo-A becomes phosphorylated at Tyr-694 in the N-terminal region. The phosphorylation is mediated co-operatively by Src-family tyrosine kinases, which play many important roles in the nervous system. Levels of tyrosine phosphorylation of Nogo-A seem to be irrelevant to developmental stages of oligodendrocytes, and might be regulated by specific extracellular stimuli. Identification of tyrosine phosphorylation of Nogo-A will introduce an additional level of complexity into Nogo-A functions.