| First Author | Yokoyama K | Year | 2006 |
| Journal | Biochem Biophys Res Commun | Volume | 349 |
| Issue | 4 | Pages | 1401-5 |
| PubMed ID | 16979591 | Mgi Jnum | J:113100 |
| Mgi Id | MGI:3664501 | Doi | 10.1016/j.bbrc.2006.09.007 |
| Citation | Yokoyama K, et al. (2006) Phosphorylation at Tyr-694 of Nogo-A by Src-family kinases. Biochem Biophys Res Commun 349(4):1401-5 |
| abstractText | 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. |
