Phosphorylation at Tyr-694 of Nogo-A by Src-family kinases.

Biochem Biophys Res Commun

Division of Oncology, Department of Cancer Biology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Tokyo 108-8639, Japan.

Published: November 2006

AI Article Synopsis

  • Nogo-A is a protein that inhibits nerve growth in the central nervous system, and its removal in mice doesn't significantly enhance nerve regeneration, indicating it may have additional roles.
  • Targeted studies revealed that Nogo-A can be phosphorylated at Tyr-694 by Src-family tyrosine kinases, which are crucial for nervous system functions.
  • This phosphorylation doesn't vary with the development of specific nerve cells (oligodendrocytes) and could be influenced by certain external signals, adding complexity to the understanding of Nogo-A's functions.

Article Abstract

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.

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http://dx.doi.org/10.1016/j.bbrc.2006.09.007DOI Listing

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