Tau interacts with src-family non-receptor tyrosine kinases

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

doi:10.1242/jcs.111.21.3167

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Tau interacts with src-family non-receptor tyrosine kinases

Journal article

Peer reviewed

Tau interacts with src-family non-receptor tyrosine kinases

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

Journal of cell science, Vol.111 (21), pp.3167-3177

11/1998

DOI: 10.1242/jcs.111.21.3167

PMID: 9763511

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Abstract

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 also resulted in an alteration in NIH3T3 cell morphology, 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 tau by fyn may also have a role in neuropathogenesis, as fyn is upregulated in Alzheimer's disease.

Phosphorylation

Signal Transduction

Transfection

Humans

Proto-Oncogene Proteins c-fyn

tau Proteins - metabolism

Recombinant Fusion Proteins - metabolism

Microtubules - metabolism

Neurites - ultrastructure

Microtubules - ultrastructure

src-Family Kinases - metabolism

Tumor Cells, Cultured

Binding Sites

Neuroblastoma - pathology

Proto-Oncogene Proteins - metabolism

Amino Acid Sequence

Actin Cytoskeleton - metabolism

Neurites - metabolism

Macromolecular Substances

Nerve Tissue Proteins - metabolism

Microscopy, Confocal

Animals

Alzheimer Disease - metabolism

Mice

Protein Processing, Post-Translational

COS Cells

3T3 Cells

Details

Title: Subtitle: Tau interacts with src-family non-receptor tyrosine kinases
Creators: Gloria Lee - Center for Neurologic Diseases, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA. gloria-lee@uiowa.edu
S Todd Newman
David L Gard
Hamid Band - Brigham and Women's Hospital
Govindaswamy Panchamoorthy
Resource Type: Journal article
Publication Details: Journal of cell science, Vol.111 (21), pp.3167-3177
Publisher: England
DOI: 10.1242/jcs.111.21.3167
PMID: 9763511
ISSN: 0021-9533
eISSN: 1477-9137
Grant note: NS32100M / NINDS NIH HHS
Language: English
Date published: 11/1998
Academic Unit: Iowa Neuroscience Institute; Immunology; Internal Medicine
Record Identifier: 9984065379202771

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