beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones.

Eyleen L K Goh, Ju Kim Young, Kenichiro Kuwako, Marc Tessier-Lavigne, Zhigang He, John W. Griffin, Guo Li Ming

Research output: Contribution to journalArticlepeer-review

57 Scopus citations


Several myelin-associated factors that inhibit axon growth of mature neurons, including Nogo66, myelin-associated glycoprotein (MAG) and oligodendrocyte myelin glycoprotein (OMgp), can associate with a common GPI-linked protein Nogo-66 receptor (NgR). Accumulating evidence suggests that myelin inhibitors also signal through unknown NgR-independent mechanisms. Here we show that MAG, a RGD tri-peptide containing protein, forms a complex with β1-integrin to mediate axonal growth cone turning responses of several neuronal types. Mutations that alter the RGD motif in MAG or inhibition of β1-integrin function, but not removal of NgRs, abolish these MAG-dependent events. In contrast, OMgp-induced repulsion is not affected by inhibition of b1-integrin function. We further show that MAG stimulates tyrosine phosphorylation of focal adhesion kinase (FAK), which in turn is required for MAG-induced growth cone turning. These studies identify β1-integrin as a specific mediator for MAG in growth cone turning responses, acting through FAK activation.

Original languageEnglish (US)
Pages (from-to)10
Number of pages1
JournalMolecular Brain
StatePublished - 2008
Externally publishedYes

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Molecular Biology


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