Tau impacts on growth-factor-stimulated actin remodeling
Autor: | Kiran Bhaskar, Joel M. Litersky, Vandana M. Sharma, Gloria Lee |
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Rok vydání: | 2007 |
Předmět: |
Fluorescent Antibody Technique
tau Proteins Transfection SH2 domain SH3 domain Receptor tyrosine kinase Mice Tubulin Chlorocebus aethiops Animals Humans Phosphorylation Cytoskeleton Platelet-Derived Growth Factor Tyrosine-protein kinase CSK biology Actin remodeling 3T3 Cells Cell Biology Molecular biology Actins Cell biology src-Family Kinases Gene Expression Regulation COS Cells biology.protein Tyrosine kinase Platelet-derived growth factor receptor Proto-oncogene tyrosine-protein kinase Src |
Zdroj: | Journal of Cell Science. 120:748-757 |
ISSN: | 1477-9137 0021-9533 |
DOI: | 10.1242/jcs.03378 |
Popis: | The microtubule-associated protein tau interacts with the SH3 domain of non-receptor Src family protein tyrosine kinases. A potential consequence of the SH3 interaction is the upregulation of tyrosine kinase activity. Here we investigated the activation of Src or Fyn by tau, both in vitro and in vivo. Tau increased the kinase activity in in vitro assays and in transfected COS7 cells. In platelet-derived growth factor (PDGF)-stimulated fibroblasts, tau appeared to prime Src for activation following PDGF stimulation, as reflected by changes in Src-mediated actin rearrangements. In addition, while fibroblasts normally recovered actin stress fibers by 5-7 hours after PDGF stimulation, tau-expressing cells showed sustained actin breakdown. Microtubule association by tau was not required for the observed changes in actin morphology. Inhibition of Src kinases or a mutant deficient in Src interaction reduced the effects, implicating Src family protein tyrosine kinases as a mediator of the effects of tau on actin rearrangements. Our results provide evidence that the interaction of tau with Src upregulates tyrosine kinase activity and that this interaction allows tau to impact on growth-factor-induced actin remodeling. |
Databáze: | OpenAIRE |
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