Tau interacts with src-family non-receptor tyrosine kinases

Gloria Lee, S. Todd Newman, David L. Gard, Hamid Band, Govindaswamy Panchamoorthy

Research output: Contribution to journalArticle

352 Scopus citations


Tau and other microtubule-associated proteins promote the assembly and stabilization of neuronal microtubules. While each microtubule-associated protein has distinct properties, their in vivo roles remain largely unknown. Tau is important in neurite outgrowth and axonal development. Recently, we showed that the amino-terminal region of tau, which is not involved in microtubule interactions, is important in NGF induced neurite outgrowth in PC12 cells. Here we report that a proline rich sequence in the amino terminus of tau interacts with the SH3 domains of fyn and src non-receptor tyrosine kinases. Tau and fyn were co-immunoprecipitated from human neuroblastoma cells and co-localization of tau and fyn was visualized in co-transfected NIH3T3 cells. Co-transfection of tau and fyn consistent with an in vivo interaction. Fyn-dependent tyrosine phosphorylation of tau occurred in transfected cells and tyrosine phosphorylated tau was identified in human neuroblastoma cells as well. Our data suggest that tau is involved in signal transduction pathways. An interaction between tau and fyn may serve as a mechanism by which extracellular signals influence the spatial distribution of microtubules. The tyrosine phosphorylation of tan by fyn may also have a role in neuropathogenesis, as fyn is upregulated in Alzheimer's disease.

Original languageEnglish (US)
Pages (from-to)3167-3177
Number of pages11
JournalJournal of cell science
Issue number21
StatePublished - Nov 1998


  • Fyn
  • SH3 domain
  • Tau
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Cell Biology

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  • Cite this

    Lee, G., Todd Newman, S., Gard, D. L., Band, H., & Panchamoorthy, G. (1998). Tau interacts with src-family non-receptor tyrosine kinases. Journal of cell science, 111(21), 3167-3177.