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Insulin Transiently Increases Tau Phosphorylation
Author(s) -
Lesort Mathieu,
Jope Richard S.,
Johnson Gail V. W.
Publication year - 1999
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1999.0720576.x
Subject(s) - phosphorylation , fyn , dephosphorylation , tyrosine phosphorylation , gsk3b , insulin , gsk 3 , medicine , endocrinology , chemistry , tyrosine , glycogen synthase , microbiology and biotechnology , biology , proto oncogene tyrosine protein kinase src , biochemistry , phosphatase
: The modulation of tau phosphorylation in response to insulin was examined in human neuroblastoma SH‐SY5Y cells. Insulin treatment resulted in a transient increase in tau phosphorylation followed by a decrease in tau phosphorylation that correlated directly with a sequential activation and deactivation of glycogen synthese kinase‐3β (GSK‐3β). The insulin‐induced increase in tau phosphorylation and concurrent activation of GSK‐3β was rapid (<2 min) and transient, and was associated with increased tyrosine phosphorylation of GSK‐3β. The increase in GSK‐3β tyrosine phosphorylation corresponded directly to an increase in the association of Fyn tyrosine kinase with GSK‐3β, and Fyn immunoprecipitated from cells treated with insulin for 1 min phosphorylated GSK‐3β to a significantly greater extent than Fyn immunoprecipitated from control cells. Subsequent to the increase in GSK‐3β activation and tau phosphorylation, treatment of cells with insulin for 60 min resulted in a dephosphorylation of tau and a decrease in GSK‐3β activity. Thus, insulin rapidly and transiently activated GSK‐3β and modulated tau phosphorylation, alterations that may contribute to neuronal plasticity.